6DEF
Vps1 GTPase-BSE fusion complexed with GMPPCP
Summary for 6DEF
| Entry DOI | 10.2210/pdb6def/pdb |
| Descriptor | Vps1 GTPase-BSE, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | vps1, vacuolar protein sorting 1, dynamin-related protein, drp, gtpase, gmppcp, endosome, vacuole, hydrolase |
| Biological source | Chaetomium thermophilum More |
| Total number of polymer chains | 4 |
| Total formula weight | 174190.35 |
| Authors | Ford, M.G.J.,Varlakhanova, N.V.,Brady, T.M.,Chappie, J.S.,Hosford, C.J. (deposition date: 2018-05-11, release date: 2018-08-22, Last modification date: 2023-10-11) |
| Primary citation | Varlakhanova, N.V.,Alvarez, F.J.D.,Brady, T.M.,Tornabene, B.A.,Hosford, C.J.,Chappie, J.S.,Zhang, P.,Ford, M.G.J. Structures of the fungal dynamin-related protein Vps1 reveal a unique, open helical architecture. J. Cell Biol., 217:3608-3624, 2018 Cited by PubMed 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. PubMed: 30087125DOI: 10.1083/jcb.201712021 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.26 Å) |
Structure validation
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