5FVK
Crystal structure of Vps4-Vfa1 complex from S.cerevisiae at 1.66 A resolution.
Summary for 5FVK
| Entry DOI | 10.2210/pdb5fvk/pdb |
| Related | 5FVL |
| Descriptor | VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 4, VPS4-ASSOCIATED PROTEIN 1 (3 entities in total) |
| Functional Keywords | hydrolase, vps4, vfa1, mit domain, yeast, atpase |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) More |
| Cellular location | Endosome membrane ; Peripheral membrane protein : P52917 Cytoplasm : P40080 |
| Total number of polymer chains | 4 |
| Total formula weight | 24089.01 |
| Authors | Kojima, R.,Obita, T.,Onoue, K.,Mizuguchi, M. (deposition date: 2016-02-09, release date: 2016-04-27, Last modification date: 2024-01-10) |
| Primary citation | Kojima, R.,Obita, T.,Onoue, K.,Mizuguchi, M. Structural Fine-Tuning of Mit Interacting Motif 2 (Mim2) and Allosteric Regulation of Escrt-III by Vps4 in Yeast. J.Mol.Biol., 428:2392-, 2016 Cited by PubMed Abstract: The endosomal sorting complex required for transport (ESCRT) facilitates roles in membrane remodeling, such as multivesicular body biogenesis, enveloped virus budding and cell division. In yeast, Vps4 plays a crucial role in intraluminal vesicle formation by disassembling ESCRT proteins. Vps4 is recruited by ESCRT-III proteins to the endosomal membrane through the interaction between the microtubule interacting and trafficking (MIT) domain of Vps4 and the C-terminal MIT-interacting motif (MIM) of ESCRT-III proteins. Here, we have determined the crystal structure of Vps4-MIT in a complex with Vps20, a member of ESCRT-III, and revealed that Vps20 adopts a unique MIM2 conformation. Based on structural comparisons with other known MIM2s, we have refined the consensus sequence of MIM2. We have shown that another ESCRT-III protein, Ist1, binds to Vps4-MIT via its C-terminal MIM1 with higher affinity than Vps2, but lacks MIM2 by surface plasmon resonance. Surprisingly, the Ist1 MIM1 competed with the MIM2 of Vfa1, a regulator of Vps4, for binding to Vps4-MIT, even though these MIMs bind in non-overlapping sites on the MIT. These findings provide insight into the allosteric recognition of MIMs of ESCRT-III by Vps4 and also the regulation of ESCRT machinery at the last step of membrane remodeling. PubMed: 27075672DOI: 10.1016/J.JMB.2016.04.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.658 Å) |
Structure validation
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