2KLY
Solution structure of human ubiquitin conjugating enzyme Ube2g2
2KLY の概要
エントリーDOI | 10.2210/pdb2kly/pdb |
NMR情報 | BMRB: 16404 |
分子名称 | Ubiquitin-conjugating enzyme E2 G2 (1 entity in total) |
機能のキーワード | alpha beta fold, atp-binding, ligase, nucleotide-binding, ubl conjugation pathway |
由来する生物種 | Homo sapiens (human) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 18777.46 |
構造登録者 | |
主引用文献 | Ju, T.,Bocik, W.,Majumdar, A.,Tolman, J.R. Solution structure and dynamics of human ubiquitin conjugating enzyme Ube2g2. Proteins, 78:1291-1301, 2010 Cited by PubMed Abstract: Ube2g2 is an E2 enzyme which functions as part of the endoplasmic reticulum-associated degradation (ERAD) pathway responsible for identification and degradation of misfolded proteins in the endoplasmic reticulum. In tandem with a cognate E3 ligase, Ube2g2 assembles K48-linked polyubiquitin chains and then transfers them to substrate, leading ultimately to proteasomal degradation of the polyubiquitin-tagged substrate. We report here the solution structure and backbone dynamics of Ube2g2 solved by nuclear magnetic resonance spectroscopy. Although the solution structure agrees well with crystallographic structures for the E2 core, catalytically important loops (encompassing residues 95-107 and 130-135) flanking the active site cysteine are poorly defined. (15)N spin relaxation and residual dipolar coupling analysis directly demonstrates that these two loops are highly dynamic in solution. These results suggest that Ube2g2 requires one or more of its protein partners, such as cognate E3, acceptor ubiquitin substrate or thiolester-linked donor ubiquitin, to assume its catalytically relevant conformation. Within the NMR structural ensemble, interactions were observed between His94 and the highly mobile loop residues Asp98 and Asp99, supporting a possible role for His94 as a general base activated by the carboxylate side-chains of Asp98 or Asp99. PubMed: 20014027DOI: 10.1002/prot.22648 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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