1i7k
From Proteopedia
|
CRYSTAL STRUCTURE OF HUMAN MITOTIC-SPECIFIC UBIQUITIN-CONJUGATING ENZYME, UBCH10
Overview
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.
About this Structure
1I7K is a Single protein structure of sequence from Homo sapiens. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.
Reference
Structural and functional analysis of the human mitotic-specific ubiquitin-conjugating enzyme, UbcH10., Lin Y, Hwang WC, Basavappa R, J Biol Chem. 2002 Jun 14;277(24):21913-21. Epub 2002 Apr 1. PMID:11927573
Page seeded by OCA on Mon Nov 12 17:27:08 2007
