Gattin, Zrinka

[["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","311"],["dc.bibliographiccitation.issue","3-4"],["dc.bibliographiccitation.journal","Journal of Biomolecular NMR"],["dc.bibliographiccitation.lastpage","320"],["dc.bibliographiccitation.volume","61"],["dc.contributor.author","Gattin, Zrinka"],["dc.contributor.author","Schneider, Robert"],["dc.contributor.author","Laukat, Yvonne"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Maier, Elke"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Benz, Roland"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Lange, Adam"],["dc.date.accessioned","2017-09-07T11:44:27Z"],["dc.date.available","2017-09-07T11:44:27Z"],["dc.date.issued","2015"],["dc.description.abstract","The voltage-dependent anion channel (VDAC) is the most abundant protein of the outer mitochondrial membrane and constitutes the major pathway for the transport of ADP, ATP, and other metabolites. In this multidisciplinary study we combined solid-state NMR, electrophysiology, and molecular dynamics simulations, to study the structure of the human VDAC isoform 2 in a lipid bilayer environment. We find that the structure of hVDAC2 is similar to the structure of hVDAC1, in line with recent investigations on zfVDAC2. However, hVDAC2 appears to exhibit an increased conformational heterogeneity compared to hVDAC1 which is reflected in broader solid-state NMR spectra and less defined electrophysiological profiles."],["dc.identifier.doi","10.1007/s10858-014-9876-5"],["dc.identifier.gro","3141930"],["dc.identifier.isi","000352711900012"],["dc.identifier.pmid","25399320"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2657"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1573-5001"],["dc.relation.issn","0925-2738"],["dc.title","Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]