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2MT5

Isolated Ring domain

2MT5 の概要
エントリーDOI10.2210/pdb2mt5/pdb
NMR情報BMRB: 25149
分子名称Anaphase-promoting complex subunit 11, ZINC ION (2 entities in total)
機能のキーワードring domain, zinc binding domain, metal binding protein
由来する生物種Homo sapiens (human)
細胞内の位置Cytoplasm : Q9NYG5
タンパク質・核酸の鎖数1
化学式量合計8246.59
構造登録者
主引用文献Brown, N.G.,Watson, E.R.,Weissmann, F.,Jarvis, M.A.,VanderLinden, R.,Grace, C.R.,Frye, J.J.,Qiao, R.,Dube, P.,Petzold, G.,Cho, S.E.,Alsharif, O.,Bao, J.,Davidson, I.F.,Zheng, J.J.,Nourse, A.,Kurinov, I.,Peters, J.M.,Stark, H.,Schulman, B.A.
Mechanism of Polyubiquitination by Human Anaphase-Promoting Complex: RING Repurposing for Ubiquitin Chain Assembly.
Mol.Cell, 56:246-260, 2014
Cited by
PubMed Abstract: Polyubiquitination by E2 and E3 enzymes is a predominant mechanism regulating protein function. Some RING E3s, including anaphase-promoting complex/cyclosome (APC), catalyze polyubiquitination by sequential reactions with two different E2s. An initiating E2 ligates ubiquitin to an E3-bound substrate. Another E2 grows a polyubiquitin chain on the ubiquitin-primed substrate through poorly defined mechanisms. Here we show that human APC's RING domain is repurposed for dual functions in polyubiquitination. The canonical RING surface activates an initiating E2-ubiquitin intermediate for substrate modification. However, APC engages and activates its specialized ubiquitin chain-elongating E2 UBE2S in ways that differ from current paradigms. During chain assembly, a distinct APC11 RING surface helps deliver a substrate-linked ubiquitin to accept another ubiquitin from UBE2S. Our data define mechanisms of APC/UBE2S-mediated polyubiquitination, reveal diverse functions of RING E3s and E2s, and provide a framework for understanding distinctive RING E3 features specifying ubiquitin chain elongation.
PubMed: 25306923
DOI: 10.1016/j.molcel.2014.09.009
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2mt5
検証レポート(詳細版)ダウンロードをダウンロード

251801

件を2026-04-08に公開中

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