Giller, Karin

[["dc.bibliographiccitation.firstpage","3115"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America : PNAS"],["dc.bibliographiccitation.lastpage","3120"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","Salvi, Michele"],["dc.contributor.author","Schomburg, Benjamin"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Graf, Sabrina"],["dc.contributor.author","Unden, Gottfried"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lange, Adam"],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2018-01-17T11:33:34Z"],["dc.date.available","2018-01-17T11:33:34Z"],["dc.date.issued","2017"],["dc.description.abstract","Bacteria use membrane-integral sensor histidine kinases (HK) to perceive stimuli and transduce signals from the environment to the cytosol. Information on how the signal is transmitted across the membrane by HKs is still scarce. Combining both liquid- and solid-state NMR, we demonstrate that structural rearrangements in the extracytoplasmic, citrate-sensing Per-Arnt-Sim (PAS) domain of HK CitA are identical for the isolated domain in solution and in a longer construct containing the membrane-embedded HK and lacking only the kinase core. We show that upon citrate binding, the PAS domain contracts, resulting in a shortening of the C-terminal β-strand. We demonstrate that this contraction of the PAS domain, which is well characterized for the isolated domain, is the signal transmitted to the transmembrane (TM) helices in a CitA construct in liposomes. Putting the extracytoplasmic PAS domain into context of the membrane-embedded CitA construct slows down citrate-binding kinetics by at least a factor of 60, confirming that TM helix motions are linked to the citrate-binding event. Our results are confirmation of a hallmark of the HK signal transduction mechanism with atomic resolution on a full-length construct lacking only the kinase core domain."],["dc.identifier.doi","10.1073/pnas.1620286114"],["dc.identifier.pmid","28265100"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11680"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1091-6490"],["dc.title","Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","276"],["dc.bibliographiccitation.issue","7402"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","+"],["dc.bibliographiccitation.volume","486"],["dc.contributor.author","Loquet, Antoine"],["dc.contributor.author","Sgourakis, Nikolaos G."],["dc.contributor.author","Gupta, Rashmi"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Goosmann, Christian"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Kolbe, Michael"],["dc.contributor.author","Baker, David"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lange, Adam"],["dc.date.accessioned","2017-09-07T11:48:51Z"],["dc.date.available","2017-09-07T11:48:51Z"],["dc.date.issued","2012"],["dc.description.abstract","Pathogenic bacteria using a type III secretion system (T3SS)(1,2) to manipulate host cells cause many different infections including Shigella dysentery, typhoid fever, enterohaemorrhagic colitis and bubonic plague. An essential part of the T3SS is a hollow needle-like protein filament through which effector proteins are injected into eukaryotic host cells(3-6). Currently, the three-dimensional structure of the needle is unknown because it is not amenable to X-ray crystallography and solution NMR, as a result of its inherent non-crystallinity and insolubility. Cryo-electron microscopy combined with crystal or solution NMR subunit structures has recently provided a powerful hybrid approach for studying supramolecular assemblies(7-12), resulting in low-resolution and medium-resolution models(13-17). However, such approaches cannot deliver atomic details, especially of the crucial subunit-subunit interfaces, because of the limited cryo-electron microscopic resolution obtained in these studies. Here we report an alternative approach combining recombinant wild-type needle production, solid-state NMR, electron microscopy and Rosetta modelling to reveal the supramolecular interfaces and ultimately the complete atomic structure of the Salmonella typhimurium T3SS needle. We show that the 80-residue subunits form a right-handed helical assembly with roughly 11 subunits per two turns, similar to that of the flagellar filament of S. typhimurium. In contrast to established models of the needle in which the amino terminus of the protein subunit was assumed to be alpha-helical and positioned inside the needle, our model reveals an extended amino-terminal domain that is positioned on the surface of the needle, while the highly conserved carboxy terminus points towards the lumen."],["dc.identifier.doi","10.1038/nature11079"],["dc.identifier.gro","3142519"],["dc.identifier.isi","000305189000039"],["dc.identifier.pmid","22699623"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8879"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.eissn","1476-4687"],["dc.relation.issn","0028-0836"],["dc.title","Atomic model of the type III secretion system needle"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1540"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Structure"],["dc.bibliographiccitation.lastpage","1549"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Schneider, Robert"],["dc.contributor.author","Briones, Rodolfo"],["dc.contributor.author","Gattin, Zrinka"],["dc.contributor.author","Demers, Jean-Philippe"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Maier, Elke"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Benz, Roland"],["dc.contributor.author","Groot, Bert L. de"],["dc.contributor.author","Lange, Adam"],["dc.date.accessioned","2017-09-07T11:48:25Z"],["dc.date.available","2017-09-07T11:48:25Z"],["dc.date.issued","2012"],["dc.description.abstract","The voltage-dependent anion channel (VDAC) is the major protein in the outer mitochondrial membrane, where it mediates transport of ATP and ADP. Changes in its permeability, induced by voltage or apoptosis-related proteins, have been implicated in apoptotic pathways. The three-dimensional structure of VDAC has recently been determined as a 19-stranded beta-barrel with an in-lying N-terminal helix. However, its gating mechanism is still unclear. Using solid-state NMR spectroscopy, molecular dynamics simulations, and electrophysiology, we show that deletion of the rigid N-terminal helix sharply increases overall motion in VDAC's beta-barrel, resulting in elliptic, semicollapsed barrel shapes. These states quantitatively reproduce conductance and selectivity of the closed VDAC conformation. Mutation of the N-terminal helix leads to a phenotype intermediate to the open and closed states. These data suggest that the N-terminal helix controls entry into elliptic beta-barrel states which underlie VDAC closure. Our results also indicate that beta-barrel channels are intrinsically flexible."],["dc.identifier.doi","10.1016/j.str.2012.06.015"],["dc.identifier.gro","3142466"],["dc.identifier.isi","000308682700013"],["dc.identifier.pmid","22841291"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8596"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cell Press"],["dc.relation.eissn","1878-4186"],["dc.relation.issn","0969-2126"],["dc.title","beta-Barrel Mobility Underlies Closure of the Voltage-Dependent Anion Channel"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13397"],["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","Journal of biological chemistry"],["dc.bibliographiccitation.lastpage","13406"],["dc.bibliographiccitation.volume","289"],["dc.contributor.author","Villinger, Saskia"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Bayrhuber, Monika"],["dc.contributor.author","Lange, Adam"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2017-09-07T11:46:15Z"],["dc.date.available","2017-09-07T11:46:15Z"],["dc.date.issued","2014"],["dc.description.abstract","Background: Human VDAC1 mediates and controls the transport of metabolites across the outer mitochondrial membrane. Results: The N-terminal helix of hVDAC1 is involved in binding to charged forms of ATP, UTP, and GTP with an important contribution from lysine 20. Conclusion: Weak binding of ATP confers specificity for ATP transport. Significance: ATP interaction mapped at residue resolution supports metabolite selectivity of VDAC. The voltage-dependent anion channel (VDAC) mediates and gates the flux of metabolites and ions across the outer mitochondrial membrane and is a key player in cellular metabolism and apoptosis. Here we characterized the binding of nucleotides to human VDAC1 (hVDAC1) on a single-residue level using NMR spectroscopy and site-directed mutagenesis. We find that hVDAC1 possesses one major binding region for ATP, UTP, and GTP that partially overlaps with a previously determined NADH binding site. This nucleotide binding region is formed by the N-terminal -helix, the linker connecting the helix to the first -strand and adjacent barrel residues. hVDAC1 preferentially binds the charged forms of ATP, providing support for a mechanism of metabolite transport in which direct binding to the charged form exerts selectivity while at the same time permeation of the Mg2+-complexed ATP form is possible."],["dc.identifier.doi","10.1074/jbc.M113.524173"],["dc.identifier.gro","3142126"],["dc.identifier.isi","000335522800038"],["dc.identifier.pmid","24668813"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4833"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.eissn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","Nucleotide Interactions of the Human Voltage-dependent Anion Channel"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1223"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","1234"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Briones, Rodolfo"],["dc.contributor.author","Weichbrodt, Conrad"],["dc.contributor.author","Paltrinieri, Licia"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Villinger, Saskia"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Lange, Adam"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","De Groot, Bert L."],["dc.date.accessioned","2017-09-07T11:44:37Z"],["dc.date.available","2017-09-07T11:44:37Z"],["dc.date.issued","2016"],["dc.description.abstract","The voltage-dependent anion channel 1 (VDAC-1) is an important protein of the outer mitochondria! membrane that transports energy metabolites and is involved in apoptosis. The available structures of VDAC proteins show a wide beta-stranded barrel pore, with its N-terminal alpha-helix (N-alpha) bound to its interior. Electrophysiology experiments revealed that voltage, its polarity, and membrane composition modulate VDAC currents. Experiments with VDAC-1 mutants identified amino acids that regulate the gating process. However, the mechanisms for how these factors regulate VDAC-1, and which changes they trigger in the channel, are still unknown. In this study, molecular dynamics simulations and single-channel experiments of VDAC-1 show agreement for the current-voltage relationships of an \"open\" channel and they also show several subconducting transient states that are more cation selective in the simulations. We observed voltage-dependent asymmetric distortions of the VDAC-1 barrel and the displacement of particular charged amino acids. We constructed conformational models of the protein voltage response and the pore changes that consistently explain the protein conformations observed at opposite voltage polarities, either in phosphatidylethanolamine or phosphatidylcholine membranes. The submicrosecond VDAC-1 voltage response shows intrinsic structural changes that explain the role of key gating amino acids and support some of the current gating hypotheses. These voltage-dependent protein changes include asymmetric barrel distortion, its interaction with the membrane, and significant displacement of N-alpha amino acids."],["dc.identifier.doi","10.1016/j.bpj.2016.08.007"],["dc.identifier.gro","3141619"],["dc.identifier.isi","000383925700015"],["dc.identifier.pmid","27653481"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13769"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1900"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Voltage Dependence of Conformational Dynamics and Subconducting States of VDAC-1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","151"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Biomolecular NMR"],["dc.bibliographiccitation.lastpage","160"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Chevelkov, Veniamin"],["dc.contributor.author","Xiang, ShengQi"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lange, Adam"],["dc.contributor.author","Reif, Bernd"],["dc.date.accessioned","2021-06-01T10:49:19Z"],["dc.date.available","2021-06-01T10:49:19Z"],["dc.date.issued","2015"],["dc.identifier.doi","10.1007/s10858-015-9902-2"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86243"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1573-5001"],["dc.relation.issn","0925-2738"],["dc.title","Perspectives for sensitivity enhancement in proton-detected solid-state NMR of highly deuterated proteins by preserving water magnetization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","22546"],["dc.bibliographiccitation.issue","52"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","22551"],["dc.bibliographiccitation.volume","107"],["dc.contributor.author","Villinger, Saskia"],["dc.contributor.author","Briones, Rodolfo"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Lange, Adam"],["dc.contributor.author","Groot, Bert L. de"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Zweckstetter, Markus"],["dc.date.accessioned","2017-09-07T11:45:10Z"],["dc.date.available","2017-09-07T11:45:10Z"],["dc.date.issued","2010"],["dc.description.abstract","The voltage-dependent anion channel (VDAC), located in the outer mitochondrial membrane, acts as a gatekeeper for the entry and exit of mitochondrial metabolites. Here we reveal functional dynamics of isoform one of VDAC (VDAC1) by a combination of solution NMR spectroscopy, Gaussian network model analysis, and molecular dynamics simulation. Micro-to millisecond dynamics are significantly increased for the N-terminal six beta-strands of VDAC1 in micellar solution, in agreement with increased B-factors observed in the same region in the bicellar crystal structure of VDAC1. Molecular dynamics simulations reveal that a charge on the membrane-facing glutamic acid 73 (E73) accounts for the elevation of N-terminal protein dynamics as well as a thinning of the nearby membrane. Mutation or chemical modification of E73 strongly reduces the micro-to millisecond dynamics in solution. Because E73 is necessary for hexokinase-I-induced VDAC channel closure and inhibition of apoptosis, our results imply that micro- to millisecond dynamics in the N-terminal part of the barrel are essential for VDAC interaction and gating."],["dc.identifier.doi","10.1073/pnas.1012310108"],["dc.identifier.gro","3142815"],["dc.identifier.isi","000285684200039"],["dc.identifier.pmid","21148773"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/261"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Functional dynamics in the voltage-dependent anion channel"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1882"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","1885"],["dc.bibliographiccitation.volume","49"],["dc.contributor.author","Schneider, Robert"],["dc.contributor.author","Etzkorn, Manuel"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Daebel, Venita"],["dc.contributor.author","Eisfeld, Joerg"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lange, Adam"],["dc.date.accessioned","2017-09-07T11:46:10Z"],["dc.date.available","2017-09-07T11:46:10Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1002/anie.200906241"],["dc.identifier.gro","3142985"],["dc.identifier.isi","000275388300034"],["dc.identifier.pmid","20140924"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/449"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.eissn","1521-3773"],["dc.relation.issn","1433-7851"],["dc.title","The Native Conformation of the Human VDAC1 N Terminus"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11691"],["dc.bibliographiccitation.issue","40"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","11695"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Habenstein, Birgit"],["dc.contributor.author","Loquet, Antoine"],["dc.contributor.author","Hwang, Songhwan"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Vasa, Suresh Kumar"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Habeck, Michael"],["dc.contributor.author","Lange, Adam"],["dc.date.accessioned","2018-11-07T09:51:27Z"],["dc.date.available","2018-11-07T09:51:27Z"],["dc.date.issued","2015"],["dc.description.abstract","Type 1 pili are filamentous protein assemblies on the surface of Gram-negative bacteria that mediate adhesion to host cells during the infection process. The molecular structure of type 1 pili remains elusive on the atomic scale owing to their insolubility and noncrystallinity. Herein we describe an approach for hybrid-structure determination that is based on data from solution-state NMR spectroscopy on the soluble subunit and solid-state NMR spectroscopy and STEM data on the assembled pilus. Our approach is based on iterative modeling driven by structural information extracted from different sources and provides a general tool to access pseudo atomic structures of protein assemblies with complex subunit folds. By using this methodology, we determined the local conformation of the FimA pilus subunit in the context of the assembled type 1 pilus, determined the exact helical pilus architecture, and elucidated the intermolecular interfaces contributing to pilus assembly and stability with atomic detail."],["dc.identifier.doi","10.1002/anie.201505065"],["dc.identifier.isi","000363394800014"],["dc.identifier.pmid","26267365"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35918"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","1521-3773"],["dc.relation.issn","1433-7851"],["dc.title","Hybrid Structure of the Type 1 Pilus of Uropathogenic Escherichia coli"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.contributor.author","Najbauer, Eszter E."],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Lange, Adam"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","de Groot, Bert L."],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Andreas, Loren B."],["dc.date.accessioned","2021-04-14T08:29:17Z"],["dc.date.available","2021-04-14T08:29:17Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1007/s00249-021-01515-7"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82857"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.title","Structure, gating and interactions of the voltage-dependent anion channel"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]