Dickmanns, Achim

[["dc.bibliographiccitation.firstpage","960"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","965"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Haselbach, David"],["dc.contributor.author","Voss, Bela"],["dc.contributor.author","Russek, Andreas"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Thomson, Emma"],["dc.contributor.author","Hurt, Ed"],["dc.contributor.author","Zachariae, Ulrich"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:48:18Z"],["dc.date.available","2017-09-07T11:48:18Z"],["dc.date.issued","2013"],["dc.description.abstract","In eukaryotes, the nucleocytoplasmic transport of macromolecules is mainly mediated by soluble nuclear transport receptors of the karyopherin-beta superfamily termed importins and exportins. The highly versatile exportin chromosome region maintenance 1 (CRM1) is essential for nuclear depletion of numerous structurally and functionally unrelated protein and ribonucleoprotein cargoes. CRM1 has been shown to adopt a toroidal structure in several functional transport complexes and was thought to maintain this conformation throughout the entire nucleocytoplasmic transport cycle. We solved crystal structures of free CRM1 from the thermophilic eukaryote Chaetomium thermophilum. Surprisingly, unbound CRM1 exhibits an overall extended and pitched superhelical conformation. The two regulatory regions, namely the acidic loop and the C-terminal a-helix, are dramatically repositioned in free CRM1 in comparison with the ternary CRM1-Ran-Snurportin1 export complex. Single-particle EM analysis demonstrates that, in a noncrystalline environment, free CRM1 exists in equilibrium between extended, superhelical and compact, ring-like conformations. Molecular dynamics simulations show that the C-terminal helix plays an important role in regulating the transition from an extended to a compact conformation and reveal how the binding site for nuclear export signals of cargoes is modulated by different CRM1 conformations. Combining these results, we propose a model for the cooperativity of CRM1 export complex assembly involving the long-range allosteric communication between the distant binding sites of GTP-bound Ran and cargo."],["dc.identifier.doi","10.1073/pnas.1215214110"],["dc.identifier.gro","3142406"],["dc.identifier.isi","000313909100042"],["dc.identifier.pmid","23277578"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7930"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Structural basis for cooperativity of CRM1 export complex formation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","102144"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.contributor.author","Heidemann, Jana L."],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Krüger, Larissa"],["dc.contributor.author","Wicke, Dennis"],["dc.contributor.author","Vinhoven, Liza"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Stülke, Jörg"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2022-07-01T07:35:47Z"],["dc.date.available","2022-07-01T07:35:47Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1016/j.jbc.2022.102144"],["dc.identifier.pii","S0021925822005865"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112267"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-581"],["dc.relation.issn","0021-9258"],["dc.title","Structural basis for c-di-AMP-dependent regulation of the bacterial stringent response by receptor protein DarB"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","785"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Structure"],["dc.bibliographiccitation.lastpage","795.e4"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2020-12-10T15:21:31Z"],["dc.date.available","2020-12-10T15:21:31Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.str.2018.03.004"],["dc.identifier.issn","0969-2126"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73053"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Validating Resolution Revolution"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","705"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Acta crystallographica. Section D, Structural biology"],["dc.bibliographiccitation.lastpage","717"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Tauchert, Marcel J."],["dc.contributor.author","Hémonnot, Clément"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Dickmanns, Achim"],["dc.date.accessioned","2020-12-10T18:26:04Z"],["dc.date.available","2020-12-10T18:26:04Z"],["dc.date.issued","2016"],["dc.description.abstract","In eukaryotic cells, the exchange of macromolecules between the nucleus and cytoplasm is highly selective and requires specialized soluble transport factors. Many of them belong to the importin-beta superfamily, the members of which share an overall superhelical structure owing to the tandem arrangement of a specific motif, the HEAT repeat. This structural organization leads to great intrinsic flexibility, which in turn is a prerequisite for the interaction with a variety of proteins and for its transport function. During the passage from the aqueous cytosol into the nucleus, the receptor passes the gated channel of the nuclear pore complex filled with a protein meshwork of unknown organization, which seems to be highly selective owing to the presence of FG-repeats, which are peptides with hydrophobic patches. Here, the structural changes of free importin-beta from a single organism, crystallized in polar (salt) or apolar (PEG) buffer conditions, are reported. This allowed analysis of the structural changes, which are attributable to the surrounding milieu and are not affected by bound interaction partners. The importin-beta structures obtained exhibit significant conformational changes and suggest an influence of the polarity of the environment, resulting in an extended conformation in the PEG condition. The significance of this observation is supported by SAXS experiments and the analysis of other crystal structures of importin-beta deposited in the Protein Data Bank."],["dc.identifier.doi","10.1107/S2059798316004940"],["dc.identifier.fs","622294"],["dc.identifier.gro","3141673"],["dc.identifier.isi","000379911500002"],["dc.identifier.issn","2059-7983"],["dc.identifier.pmid","27303791"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75940"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2059-7983"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","molecular biophysics"],["dc.title","Impact of the crystallization condition on importin-β conformation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1678"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Structure"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2022-03-01T11:45:23Z"],["dc.date.available","2022-03-01T11:45:23Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/j.str.2018.10.028"],["dc.identifier.pii","S0969212618303897"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103311"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0969-2126"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Validating Resolution Revolution"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1001750"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLoS Biology"],["dc.bibliographiccitation.lastpage","15"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Ahmed, Yasar Luqman"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Park, Hee-Soo"],["dc.contributor.author","Bayram, Ozgür"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ni, Min"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Kim, Sun Chang"],["dc.contributor.author","Yu, Jae-Hyuk"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:47:00Z"],["dc.date.available","2017-09-07T11:47:00Z"],["dc.date.issued","2013"],["dc.description.abstract","Morphological development of fungi and their combined production of secondary metabolites are both acting in defence and protection. These processes are mainly coordinated by velvet regulators, which contain a yet functionally and structurally uncharacterized velvet domain. Here we demonstrate that the velvet domain of VosA is a novel DNA-binding motif that specifically recognizes an 11-nucleotide consensus sequence consisting of two motifs in the promoters of key developmental regulatory genes. The crystal structure analysis of the VosA velvet domain revealed an unforeseen structural similarity with the Rel homology domain (RHD) of the mammalian transcription factor NF-B. Based on this structural similarity several conserved amino acid residues present in all velvet domains have been identified and shown to be essential for the DNA binding ability of VosA. The velvet domain is also involved in dimer formation as seen in the solved crystal structures of the VosA homodimer and the VosA-VelB heterodimer. These findings suggest that defence mechanisms of both fungi and animals might be governed by structurally related DNA-binding transcription factors."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2013"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2014"],["dc.identifier.doi","10.1371/journal.pbio.1001750"],["dc.identifier.gro","3142241"],["dc.identifier.isi","000329367200028"],["dc.identifier.pmid","24391470"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9579"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6098"],["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.issn","1545-7885"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","The Velvet Family of Fungal Regulators Contains a DNA-Binding Domain Structurally Similar to NF-κB"],["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","1087"],["dc.bibliographiccitation.issue","5930"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","1091"],["dc.bibliographiccitation.volume","324"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Guettler, Thomas"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Goerlich, Dirk"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:47:28Z"],["dc.date.available","2017-09-07T11:47:28Z"],["dc.date.issued","2009"],["dc.description.abstract","CRM1 mediates nuclear export of numerous unrelated cargoes, which may carry a short leucine-rich nuclear export signal or export signatures that include folded domains. How CRM1 recognizes such a variety of cargoes has been unknown up to this point. Here we present the crystal structure of the SPN1.CRM1.RanGTP export complex at 2.5 angstrom resolution (where SPN1 is snurportin1 and RanGTP is guanosine 5' triphosphate-bound Ran). SPN1 is a nuclear import adapter for cytoplasmically assembled, m(3)G-capped spliceosomal U snRNPs (small nuclear ribonucleoproteins). The structure shows how CRM1 can specifically return the cargo-free form of SPN1 to the cytoplasm. The extensive contact area includes five hydrophobic residues at the SPN1 amino terminus that dock into a hydrophobic cleft of CRM1, as well as numerous hydrophilic contacts of CRM1 to m3G cap-binding domain and carboxyl-terminal residues of SPN1. The structure suggests that RanGTP promotes cargo-binding to CRM1 solely through long-range conformational changes in the exportin."],["dc.identifier.doi","10.1126/science.1173388"],["dc.identifier.gro","3143116"],["dc.identifier.isi","000266246700046"],["dc.identifier.pmid","19389996"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/595"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Assoc Advancement Science"],["dc.relation.issn","0036-8075"],["dc.title","Crystal Structure of the Nuclear Export Receptor CRM1 in Complex with Snurportin1 and RanGTP"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1251"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLANT PHYSIOLOGY"],["dc.bibliographiccitation.lastpage","1266"],["dc.bibliographiccitation.volume","160"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Brodhun, Florian"],["dc.contributor.author","Sauer, Kristin"],["dc.contributor.author","Herrfurth, Cornelia"],["dc.contributor.author","Hamberg, Mats"],["dc.contributor.author","Brinkmann, Jens"],["dc.contributor.author","Scholz, Julia"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:48:22Z"],["dc.date.available","2017-09-07T11:48:22Z"],["dc.date.issued","2012"],["dc.description.abstract","In plants, oxylipins regulate developmental processes and defense responses. The first specific step in the biosynthesis of the cyclopentanone class of oxylipins is catalyzed by allene oxide cyclase (AOC) that forms cis(+)-12-oxo-phytodienoic acid. The moss Physcomitrella patens has two AOCs (PpAOC1 and PpAOC2) with different substrate specificities for C-18- and C-20-derived substrates, respectively. To better understand AOC's catalytic mechanism and to elucidate the structural properties that explain the differences in substrate specificity, we solved and analyzed the crystal structures of 36 monomers of both apo and ligand complexes of PpAOC1 and PpAOC2. From these data, we propose the following intermediates in AOC catalysis: (1) a resting state of the apo enzyme with a closed conformation, (2) a first shallow binding mode, followed by (3) a tight binding of the substrate accompanied by conformational changes in the binding pocket, and (4) initiation of the catalytic cycle by opening of the epoxide ring. As expected, the substrate dihydro analog cis-12,13S-epoxy-9Z,15Z-octadecadienoic acid did not cyclize in the presence of PpAOC1; however, when bound to the enzyme, it underwent isomerization into the corresponding trans-epoxide. By comparing complex structures of the C-18 substrate analog with in silico modeling of the C-20 substrate analog bound to the enzyme allowed us to identify three major molecular determinants responsible for the different substrate specificities (i.e. larger active site diameter, an elongated cavity of PpAOC2, and two nonidentical residues at the entrance of the active site)."],["dc.identifier.doi","10.1104/pp.112.205138"],["dc.identifier.gro","3142446"],["dc.identifier.isi","000310584200009"],["dc.identifier.pmid","22987885"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8374"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0032-0889"],["dc.title","Crystal Structures of Physcomitrella patens AOC1 and AOC2: Insights into the Enzyme Mechanism and Differences in Substrate Specificity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","10463"],["dc.bibliographiccitation.issue","27"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","10470"],["dc.bibliographiccitation.volume","294"],["dc.contributor.author","Heidemann, Jana L."],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2020-12-10T18:12:59Z"],["dc.date.available","2020-12-10T18:12:59Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1074/jbc.RA119.009246"],["dc.identifier.eissn","1083-351X"],["dc.identifier.issn","0021-9258"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74549"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Crystal structures of the c-di-AMP–synthesizing enzyme CdaA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7545"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Journal of Medicinal Chemistry"],["dc.bibliographiccitation.lastpage","7558"],["dc.bibliographiccitation.volume","63"],["dc.contributor.author","Shaikhqasem, Alaa"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2021-04-14T08:24:31Z"],["dc.date.available","2021-04-14T08:24:31Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1021/acs.jmedchem.0c00143"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81316"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1520-4804"],["dc.relation.issn","0022-2623"],["dc.title","Characterization of Inhibition Reveals Distinctive Properties for Human and Saccharomyces cerevisiae CRM1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]