Ficner, Ralf

[["dc.bibliographiccitation.firstpage","s30"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica Section A Foundations and Advances"],["dc.bibliographiccitation.lastpage","s30"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Port, Sarah A."],["dc.contributor.author","Weiß, Manfred S."],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.contributor.author","Dickmanns, Achim"],["dc.date.accessioned","2020-12-10T18:26:02Z"],["dc.date.available","2020-12-10T18:26:02Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1107/S2053273316099526"],["dc.identifier.issn","2053-2733"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75925"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.title","Crystal structure of the 239 kDa nuclear export complex CRM1 - RanGTP - Snurportin1 - Nup214 - MBP"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["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","c59"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica Section A Foundations of Crystallography"],["dc.bibliographiccitation.lastpage","c60"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Strasser, A."],["dc.contributor.author","Dickmanns, A."],["dc.contributor.author","Lührmann, R."],["dc.date.accessioned","2022-03-01T11:47:02Z"],["dc.date.available","2022-03-01T11:47:02Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1107/S0108767305097473"],["dc.identifier.pii","S0108767305097473"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103890"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0108-7673"],["dc.title","Structural basis for specific recognition of the UsnRNP m 3 G-cap by snurportin1"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1481"],["dc.bibliographiccitation.journal","Acta Crystallographica Section F Structural Biology Communications"],["dc.bibliographiccitation.lastpage","1487"],["dc.bibliographiccitation.volume","71"],["dc.contributor.author","Monecke, Thomas"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Weiss, Manfred S."],["dc.contributor.author","Port, Sarah A."],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:54:49Z"],["dc.date.available","2017-09-07T11:54:49Z"],["dc.date.issued","2015"],["dc.description.abstract","High conformational flexibility is an intrinsic and indispensable property of nuclear transport receptors, which makes crystallization and structure determination of macromolecular complexes containing exportins or importins particularly challenging. Here, the crystallization and structure determination of a quaternary nuclear export complex consisting of the exportin CRM1, the small GTPase Ran in its GTP-bound form, the export cargo SPN1 and an FG repeat-containing fragment of the nuclear pore complex component nucleoporin Nup214 fused to maltose-binding protein is reported. Optimization of constructs, seeding and the development of a sophisticated protocol including successive PEG-mediated crystal dehydration as well as additional post-mounting steps were essential to obtain well diffracting crystals."],["dc.identifier.doi","10.1107/S2053230X15021524"],["dc.identifier.gro","3141769"],["dc.identifier.isi","000369376500007"],["dc.identifier.pmid","26625290"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/868"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [Sonderforschungsbereich SFB860]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Int Union Crystallography"],["dc.relation.issn","2053-230X"],["dc.title","Combining dehydration, construct optimization and improved data collection to solve the crystal structure of a CRM1-RanGTP-SPN1-Nup214 quaternary nuclear export complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","541"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","552"],["dc.bibliographiccitation.volume","121"],["dc.contributor.author","Dierks, T."],["dc.contributor.author","Dickmanns, A."],["dc.contributor.author","Preusser-Kunze, A."],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Mariappan, M."],["dc.contributor.author","Von Figura, K."],["dc.contributor.author","Ficner, R."],["dc.contributor.author","Rudolph, M."],["dc.date.accessioned","2017-09-07T11:54:25Z"],["dc.date.available","2017-09-07T11:54:25Z"],["dc.date.issued","2005"],["dc.description.abstract","Sulfatases are enzymes essential for degradation and remodeling of sulfate esters. Formylglycine (FGly), the key catalytic residue in the active site, is unique to sulfatases. In higher eukaryotes, FGly is generated from a cysteine precursor by the FGly-generating enzyme (FGE). Inactivity of FGE results in multiple sulfatase deficiency (MSD), a fatal autosomal recessive syndrome. Based on the crystal structure, we report that FGE is a single-domain monomer with a surprising paucity of secondary structure and adopts a unique fold. The effect of all 18 missense mutations found in MSD patients is explained by the FGE structure, providing a molecular basis of MSD. The catalytic mechanism of FGly generation was elucidated by six high-resolution structures of FGE in different redox environments. The structures allow formulation of a novel oxygenase mechanism whereby FGE utilizes molecular oxygen to generate FGly via a cysteine sulfenic acid intermediate."],["dc.identifier.doi","10.1016/j.cell.2005.03.001"],["dc.identifier.gro","3143846"],["dc.identifier.isi","000229331200011"],["dc.identifier.pmid","15907468"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3452"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1405"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0092-8674"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme"],["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","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","83"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","97"],["dc.bibliographiccitation.volume","393"],["dc.contributor.author","Oschlies, Melanie"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Haselhorst, Thomas"],["dc.contributor.author","Schaper, Wiebke"],["dc.contributor.author","Stummeyer, Katharina"],["dc.contributor.author","Tiralongo, Joe"],["dc.contributor.author","Weinhold, Birgit"],["dc.contributor.author","Gerardy-Schahn, Rita"],["dc.contributor.author","von Itzstein, Mark"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Muenster-Kuehnel, Anja-K."],["dc.date.accessioned","2017-09-07T11:46:48Z"],["dc.date.available","2017-09-07T11:46:48Z"],["dc.date.issued","2009"],["dc.description.abstract","The biosynthesis of sialic acid-containing glycoconjugates is crucial for the development of vertebrate life. Cytidine monophosphate-sialic acid synthetase (CSS) catalyzes the metabolic activation of sialic acids. In vertebrates, the enzyme is chimeric, with the N-terminal domain harboring the synthetase activity. The function of the highly conserved C-terminal domain (CSS-CT) is unknown. To shed light on its biological function, we solved the X-ray structure of murine CSS-CT to 1.9 angstrom resolution. CSS-CT is a stable shamrock-like tetramer that superimposes well with phosphatases of the haloacid dehalogenase superfamily. However, a region found exclusively in vertebrate CSS-CT appears to block the active-site entrance. Accordingly, no phosphatase activity was observed in vitro, which points toward a nonenzymatic function of CSS-CT. A computational three-dimensional model of full-length CSS, in combination with in vitro oligomerization studies, provides evidence that CSS-CT serves as a platform for the quaternary organization governing the kinetic properties of the physiologically active enzyme as demonstrated in kinetic studies. (C) 2009 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.jmb.2009.08.003"],["dc.identifier.gro","3143039"],["dc.identifier.isi","000271341400007"],["dc.identifier.pmid","19666032"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/509"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Academic Press Ltd- Elsevier Science Ltd"],["dc.relation.eissn","1089-8638"],["dc.relation.issn","0022-2836"],["dc.title","A C-Terminal Phosphatase Module Conserved in Vertebrate CMP-Sialic Acid Synthetases Provides a Tetramerization Interface for the Physiologically Active Enzyme"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","861"],["dc.bibliographiccitation.journal","Acta Crystallographica Section F Structural Biology and Crystallization Communications"],["dc.bibliographiccitation.lastpage","863"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Andrade, S."],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Ficner, R."],["dc.contributor.author","Einsle, O."],["dc.date.accessioned","2017-09-07T11:54:18Z"],["dc.date.available","2017-09-07T11:54:18Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1107/S1744309105027004"],["dc.identifier.gro","3143806"],["dc.identifier.isi","000232354200016"],["dc.identifier.pmid","16511180"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1361"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1744-3091"],["dc.title","Expression, purification and crystallization of the ammonium transporter Amt-1 from Archaeoglobus fulgidus"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["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"]]