1I7K

CRYSTAL STRUCTURE OF HUMAN MITOTIC-SPECIFIC UBIQUITIN-CONJUGATING ENZYME, UBCH10

1I7K の概要

• エントリーDOI: 10.2210/pdb1i7k/pdb
• 分子名称: UBIQUITIN-CONJUGATING ENZYME E2 H10 (2 entities in total)
• 機能のキーワード: ubiquitin conjugating enzyme, ligase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39314.39

構造登録者

Basavappa, R.,Lin, Y. (登録日: 2001-03-09, 公開日: 2001-04-04, 最終更新日: 2023-08-09)

主引用文献

Lin, Y.,Hwang, W.C.,Basavappa, R.
Structural and functional analysis of the human mitotic-specific ubiquitin-conjugating enzyme, UbcH10.
J.Biol.Chem., 277:21913-21921, 2002

PubMed Abstract: Cell cycle progression is controlled at several different junctures by the targeted destruction of cell cycle regulatory proteins. These carefully orchestrated events include the destruction of the securin protein to permit entry into anaphase, and the destruction of cyclin B to permit exit from mitosis. These destruction events are mediated by the ubiquitin/proteasome system. The human ubiquitin-conjugating enzyme, UbcH10, is an essential mediator of the mitotic destruction events. We report here the 1.95-A crystal structure of a mutant UbcH10, in which the active site cysteine has been replaced with a serine. Functional analysis indicates that the mutant is active in accepting ubiquitin, although not as efficiently as wild-type. Examination of the crystal structure reveals that the NH2-terminal extension in UbcH10 is disordered and that a conserved 3(10)-helix places a lysine residue near the active site. Analysis of relevant mutants demonstrates that for ubiquitin-adduct formation the presence or absence of the NH2-terminal extension has little effect, whereas the lysine residue near the active site has significant effect. The structure provides additional insight into UbcH10 function including possible sites of interaction with the anaphase promoting complex/cyclosome and the disposition of a putative destruction box motif in the structure.

PubMed: 11927573
DOI: 10.1074/jbc.M109398200

実験手法

X-RAY DIFFRACTION (1.95 Å)