2QP9

Crystal Structure of S.cerevisiae Vps4

2QP9 の概要

• エントリーDOI: 10.2210/pdb2qp9/pdb
• 関連するPDBエントリー: 2QPA
• 分子名称: Vacuolar protein sorting-associated protein 4, CADMIUM ION, SULFATE ION (3 entities in total)
• 機能のキーワード: atpase domain, beta domain, c-terminal helix, atp-binding, endosome, nucleotide-binding, protein transport, transport, vacuole
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Endosome membrane ; Peripheral membrane protein : P52917
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39098.39

構造登録者

Xiao, J.,Xu, Z. (登録日: 2007-07-23, 公開日: 2007-10-09, 最終更新日: 2024-02-21)

主引用文献

Xiao, J.,Xia, H.,Yoshino-Koh, K.,Zhou, J.,Xu, Z.
Structural characterization of the ATPase reaction cycle of endosomal AAA protein Vps4.
J.Mol.Biol., 374:655-670, 2007

PubMed Abstract: The multivesicular body (MVB) pathway functions in multiple cellular processes including cell surface receptor down-regulation and viral budding from host cells. An important step in the MVB pathway is the correct sorting of cargo molecules, which requires the assembly and disassembly of endosomal sorting complexes required for transport (ESCRTs) on the endosomal membrane. Disassembly of the ESCRTs is catalyzed by ATPase associated with various cellular activities (AAA) protein Vps4. Vps4 contains a single AAA domain and undergoes ATP-dependent quaternary structural change to disassemble the ESCRTs. Structural and biochemical analyses of the Vps4 ATPase reaction cycle are reported here. Crystal structures of Saccharomyces cerevisiae Vps4 in both the nucleotide-free form and the ADP-bound form provide the first structural view illustrating how nucleotide binding might induce conformational changes within Vps4 that lead to oligomerization and binding to its substrate ESCRT-III subunits. In contrast to previous models, characterization of the Vps4 structure now supports a model where the ground state of Vps4 in the ATPase reaction cycle is predominantly a monomer and the activated state is a dodecamer. Comparison with a previously reported human VPS4B structure suggests that Vps4 functions in the MVB pathway via a highly conserved mechanism supported by similar protein-protein interactions during its ATPase reaction cycle.

PubMed: 17949747
DOI: 10.1016/j.jmb.2007.09.067

実験手法

X-RAY DIFFRACTION (2.9 Å)