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5FVK

Crystal structure of Vps4-Vfa1 complex from S.cerevisiae at 1.66 A resolution.

5FVK の概要
エントリーDOI10.2210/pdb5fvk/pdb
関連するPDBエントリー5FVL
分子名称VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 4, VPS4-ASSOCIATED PROTEIN 1 (3 entities in total)
機能のキーワードhydrolase, vps4, vfa1, mit domain, yeast, atpase
由来する生物種SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
詳細
細胞内の位置Endosome membrane ; Peripheral membrane protein : P52917
Cytoplasm : P40080
タンパク質・核酸の鎖数4
化学式量合計24089.01
構造登録者
Kojima, R.,Obita, T.,Onoue, K.,Mizuguchi, M. (登録日: 2016-02-09, 公開日: 2016-04-27, 最終更新日: 2024-01-10)
主引用文献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: 27075672
DOI: 10.1016/J.JMB.2016.04.007
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.658 Å)
構造検証レポート
Validation report summary of 5fvk
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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