2ZD7

The structure of VPS75 (Vacuolar protein sorting-associated protein 75)

2ZD7 の概要

• エントリーDOI: 10.2210/pdb2zd7/pdb
• 分子名称: Vacuolar protein sorting-associated protein 75, EVDLPLSDEEPSS (3 entities in total)
• 機能のキーワード: histone chaperone, vps75, nap1, nucleus, phosphoprotein, protein transport, transport
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 62728.61

構造登録者

Park, Y.J.,Luger, K. (登録日: 2007-11-20, 公開日: 2008-08-12, 最終更新日: 2024-03-13)

主引用文献

Park, Y.J.,Sudhoff, K.B.,Andrews, A.J.,Stargell, L.A.,Luger, K.
Histone chaperone specificity in Rtt109 activation.
Nat.Struct.Mol.Biol., 15:957-964, 2008

PubMed Abstract: Rtt109 is a histone acetyltransferase that requires a histone chaperone for the acetylation of histone 3 at lysine 56 (H3K56). Rtt109 forms a complex with the chaperone Vps75 in vivo and is implicated in DNA replication and repair. Here we show that both Rtt109 and Vps75 bind histones with high affinity, but only the complex is efficient for catalysis. The C-terminal acidic domain of Vps75 contributes to activation of Rtt109 and is necessary for in vivo functionality of Vps75, but it is not required for interaction with either Rtt109 or histones. We demonstrate that Vps75 is a structural homolog of yeast Nap1 by solving its crystal structure. Nap1 and Vps75 interact with histones and Rtt109 with comparable affinities. However, only Vps75 stimulates Rtt109 enzymatic activity. Our data highlight the functional specificity of Vps75 in Rtt109 activation.

PubMed: 19172749
DOI: 10.1038/nsmb.1480

実験手法

X-RAY DIFFRACTION (1.85 Å)