Au, S. W., Leng, X., Harper, J. W., Barford, D. (2002) Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10Subunit. JOURNAL OF MOLECULAR BIOLOGY, 316 (4). pp. 955-968. ISSN 0022-2836

Full text not available from this repository.

Abstract

Implications for the ubiquitination reaction of the anaphase-promoting complex from the crystal structure of the Doc1/Apc10Subunit. 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 ubiquintation activity is Doc1/Apc10, a protein composed of Doc1 homology domain that has been indentified 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 XRCC1. Residues that are invariant amongst Doc1/Apc10 sequences, including a temperature-sensitive mitotic arrest mutant, map 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 indentification 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 ligase.

Item Type:	Article
Authors (ICR Faculty only):	Barford, David
All Authors:	Au, S. W., Leng, X., Harper, J. W., Barford, D.
Research teams:	Closed research groups > Macromolecular Structure Laboratory - Barford Group
Depositing User:	EPrints Services
Date Deposited:	10 Aug 2007 20:39
Last Modified:	02 Apr 2015 09:12
URI:	http://publications.icr.ac.uk/id/eprint/913

Actions (login required)

View Item