1Z2X

Crystal structure of mouse Vps29

1Z2X の概要

• エントリーDOI: 10.2210/pdb1z2x/pdb
• 関連するPDBエントリー: 1S3M 1S3N 1Z2W
• 分子名称: Vacuolar protein sorting 29 (2 entities in total)
• 機能のキーワード: vps29, retromer, phosphatase, protein transport
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm (By similarity): Q9QZ88
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43253.66

構造登録者

Collins, B.M.,Skinner, C.F.,Watson, P.J.,Seaman, M.N.J.,Owen, D.J. (登録日: 2005-03-10, 公開日: 2005-06-21, 最終更新日: 2024-03-13)

主引用文献

Collins, B.M.,Skinner, C.F.,Watson, P.J.,Seaman, M.N.J.,Owen, D.J.
Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly
NAT.STRUCT.MOL.BIOL., 12:594-602, 2005

PubMed Abstract: The retromer complex is responsible for the retrieval of mannose 6-phosphate receptors from the endosomal system to the Golgi. Here we present the crystal structure of the mammalian retromer subunit mVps29 and show that it has structural similarity to divalent metal-containing phosphoesterases. mVps29 can coordinate metals in a similar manner but has no detectable phosphoesterase activity in vitro, suggesting a unique specificity or function. The mVps29 and mVps26 subunits bind independently to mVps35 and together form a high-affinity heterotrimeric subcomplex. Mutagenesis reveals the structural basis for the interaction of mVps29 with mVps35 and subsequent association with endosomal membranes in vivo. A conserved hydrophobic surface distinct from the primary Vps35p binding site mediates assembly of the Vps29p-Vps26p-Vps35p subcomplex with sorting nexins in yeast, and mutation of either site results in a defect in retromer-dependent membrane trafficking.

PubMed: 15965486
DOI: 10.1038/nsmb954

実験手法

X-RAY DIFFRACTION (2.22 Å)