2LUH

NMR structure of the Vta1-Vps60 complex

2LUH の概要

• エントリーDOI: 10.2210/pdb2luh/pdb
• NMR情報: BMRB: 18521
• 分子名称: Vacuolar protein sorting-associated protein VTA1, Vacuolar protein-sorting-associated protein 60 (2 entities in total)
• 機能のキーワード: vta1, vps60, escrt, mvb, novel mit recognition mode, protein transport, endocytosis
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Cytoplasm: Q06263; Endosome membrane; Peripheral membrane protein: Q03390
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25671.14

構造登録者

Yang, Z.,Vild, C.,Ju, J.,Zhang, X.,Liu, J.,Shen, J.,Zhao, B.,Lan, W.,Gong, F.,Liu, M.,Cao, C.,Xu, Z. (登録日: 2012-06-13, 公開日: 2012-11-07, 最終更新日: 2024-05-15)

主引用文献

Yang, Z.,Vild, C.,Ju, J.,Zhang, X.,Liu, J.,Shen, J.,Zhao, B.,Lan, W.,Gong, F.,Liu, M.,Cao, C.,Xu, Z.
Structural Basis of Molecular Recognition between ESCRT-III-like Protein Vps60 and AAA-ATPase Regulator Vta1 in the Multivesicular Body Pathway.
J.Biol.Chem., 287:43899-43908, 2012

PubMed Abstract: The AAA-ATPase Vps4 is critical for function of the multivesicular body sorting pathway, which impacts cellular phenomena ranging from receptor down-regulation to viral budding to cytokinesis. Vps4 activity is stimulated by the interaction between Vta1 and Vps60, but the structural basis for this interaction is unclear. The fragment Vps60(128-186) was reported to display the full activity of Vps60. Vta1 interacts with Vps60 using its N-terminal domain (Vta1NTD). In this work, the structure of Vps60(128-186) in complex with Vta1NTD was determined using NMR techniques, demonstrating a novel recognition mode of the microtubule-interacting and transport (MIT) domain in which Vps60(128-186) interacts with Vta1NTD through helices α4' and α5', extending over Vta1NTD MIT2 domain helices 1-3. The Vps60 binding does not result in Vta1 conformational changes, further revealing the fact that Vps4 ATPase is enhanced by the interaction between Vta1 and Vps60 in an unanticipated manner.

PubMed: 23105107
DOI: 10.1074/jbc.M112.390724

実験手法

SOLUTION NMR