1gqp

From Proteopedia

Revision as of 14:07, 20 November 2007

APC10/DOC1 SUBUNIT OF S. CEREVISIAE

Overview

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 Doc1/Apc10 at 2.2A resolution. The, Doc1 homology domain forms a beta-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 beta-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 colocalise 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.

About this Structure

1GQP is a Single protein structure of sequence from Saccharomyces cerevisiae with BR as ligand. Full crystallographic information is available from OCA.

Reference

Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10 subunit., Au SW, Leng X, Harper JW, Barford D, J Mol Biol. 2002 Mar 1;316(4):955-68. PMID:11884135

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