5AGC
Crystallographic forms of the Vps75 tetramer
5AGC の概要
エントリーDOI | 10.2210/pdb5agc/pdb |
分子名称 | VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 75 (1 entity in total) |
機能のキーワード | transport protein, vps75, vacuolar protein sorting 75, histone chaperone, nap1, chromatin |
由来する生物種 | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
細胞内の位置 | Nucleus : P53853 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 122624.34 |
構造登録者 | Hammond, C.M.,Sundaramoorthy, R.,Owen-Hughes, T. (登録日: 2015-01-29, 公開日: 2016-03-02, 最終更新日: 2024-01-10) |
主引用文献 | Hammond, C.M.,Sundaramoorthy, R.,Larance, M.,Lamond, A.,Stevens, M.A.,El-Mkami, H.,Norman, D.G.,Owen-Hughes, T. The Histone Chaperone Vps75 Forms Multiple Oligomeric Assemblies Capable of Mediating Exchange between Histone H3-H4 Tetramers and Asf1-H3-H4 Complexes. Nucleic Acids Res., 44:6157-, 2016 Cited by PubMed Abstract: Vps75 is a histone chaperone that has been historically characterized as homodimer by X-ray crystallography. In this study, we present a crystal structure containing two related tetrameric forms of Vps75 within the crystal lattice. We show Vps75 associates with histones in multiple oligomers. In the presence of equimolar H3-H4 and Vps75, the major species is a reconfigured Vps75 tetramer bound to a histone H3-H4 tetramer. However, in the presence of excess histones, a Vps75 dimer bound to a histone H3-H4 tetramer predominates. We show the Vps75-H3-H4 interaction is compatible with the histone chaperone Asf1 and deduce a structural model of the Vps75-Asf1-H3-H4 (VAH) co-chaperone complex using the Pulsed Electron-electron Double Resonance (PELDOR) technique and cross-linking MS/MS distance restraints. The model provides a molecular basis for the involvement of both Vps75 and Asf1 in Rtt109 catalysed histone H3 K9 acetylation. In the absence of Asf1 this model can be used to generate a complex consisting of a reconfigured Vps75 tetramer bound to a H3-H4 tetramer. This provides a structural explanation for many of the complexes detected biochemically and illustrates the ability of Vps75 to interact with dimeric or tetrameric H3-H4 using the same interaction surface. PubMed: 27036862DOI: 10.1093/NAR/GKW209 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (4 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
