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Instruments / Technical Area	Publication Details	Published	Actions
Krios I-Titan Krios I at Diamond	Structures of the fungal dynamin-related protein Vps1 reveal a unique, open helical architecture Natalia V. Varlakhanova , Frances J. D. Alvarez , Tyler M. Brady , Bryan A. Tornabene , Christopher J. Hosford , Joshua S. Chappie , Peijun Zhang , Marijn G. J. Ford The Journal Of Cell Biology 14 DOI: 10.1083/jcb.201712021 Diamond Proposal Number(s): [14856] Show Abstract ▼ Abstract: Dynamin-related proteins (DRPs) are large multidomain GTPases required for diverse membrane-remodeling events. DRPs self-assemble into helical structures, but how these structures are tailored to their cellular targets remains unclear. We demonstrate that the fungal DRP Vps1 primarily localizes to and functions at the endosomal compartment. We present crystal structures of a Vps1 GTPase–bundle signaling element (BSE) fusion in different nucleotide states to capture GTP hydrolysis intermediates and concomitant conformational changes. Using cryoEM, we determined the structure of full-length GMPPCP-bound Vps1. The Vps1 helix is more open and flexible than that of dynamin. This is due to further opening of the BSEs away from the GTPase domains. A novel interface between adjacent GTPase domains forms in Vps1 instead of the contacts between the BSE and adjacent stalks and GTPase domains as seen in dynamin. Disruption of this interface abolishes Vps1 function in vivo. Hence, Vps1 exhibits a unique helical architecture, highlighting structural flexibilities of DRP self-assembly.	Aug 2018
I03-Macromolecular Crystallography	Structures of the yeast dynamin-like GTPase Sey1p provide insight into homotypic ER fusion L. Yan , S. Sun , W. Wang , J. Shi , X. Hu , S. Wang , D. Su , Z. Rao , J. Hu , Z. Lou The Journal Of Cell Biology 210 (6), 961 - 972 DOI: 10.1083/jcb.201502078 PMID: 26370501 Open Access Show Abstract ▼ Abstract: Homotypic membrane fusion of the endoplasmic reticulum is mediated by dynamin-like guanosine triphosphatases (GTPases), which include atlastin (ATL) in metazoans and Sey1p in yeast. In this paper, we determined the crystal structures of the cytosolic domain of Sey1p derived from Candida albicans. The structures reveal a stalk-like, helical bundle domain following the GTPase, which represents a previously unidentified configuration of the dynamin superfamily. This domain is significantly longer than that of ATL and critical for fusion. Sey1p forms a side-by-side dimer in complex with GMP-PNP or GDP/AlF4− but is monomeric with GDP. Surprisingly, Sey1p could mediate fusion without GTP hydrolysis, even though fusion was much more efficient with GTP. Sey1p was able to replace ATL in mammalian cells, and the punctate localization of Sey1p was dependent on its GTPase activity. Despite the common function of fusogenic GTPases, our results reveal unique features of Sey1p.	Sep 2015

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