Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit

被引:40
作者
Au, SWN
Leng, XH
Harper, JW
Barford, D
机构
[1] Inst Canc Res, Sect Struct Biol, Chester Beatty Labs, London SW3 6JB, England
[2] Baylor Coll Med, Dept Biochem & Mol Biol, Houston, TX 77030 USA
关键词
Doc1-Apc10; APC-cyclosome; ubiquitination; E3 ubiquitin ligase; protein structure;
D O I
10.1006/jmbi.2002.5399
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The anaphase-promoting complex (APC) is a multi-subunit E3 protein ubiquitin ligase that is responsible for the metaphase to anaphase transition and the exit from mitosis. One of the subunits of the APC that is required for its ubiquitination activity is Doc1/Apc10, a protein composed of a Doc1 homology domain that has been identified in a number of diverse putative E3 ubiquitin ligases. Here, we present the crystal structure of Saccharomyces cerevisiae Doc21/Apc10 at 2.2 Angstrom resolution. The Doc1 homology domain forms a P-sandwich structure that is related in architecture to the galactose-binding domain of galactose oxidase, the coagulation factor C2 domain and a domain of XRCC1. Residues that are invariant amongst Doc1/Apc10 sequences, including a temperature-sensitive mitotic arrest mutant, map to a P-sheet region of the molecule, whose counterpart in galactose oxidase, the coagulation factor C2 domains and XRCC1 mediate bio-molecular interactions. This finding suggests the identification of the functionally important and conserved region of Doc1/Apc10 and, since invariant residues of Doc1/Apc10 colo-calise with conserved residues of other Doc1 homology domains, we propose that the Doc1 homology domains perform common ubiquitination functions in the APC and other E3 ubiquitin ligases. (C) 2002 Elsevier Science Ltd.
引用
收藏
页码:955 / 968
页数:14
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