1GQP

APC10/DOC1 SUBUNIT OF S. cerevisiae

Summary for 1GQP

• Entry DOI: 10.2210/pdb1gqp/pdb
• Descriptor: DOC1/APC10, BROMIDE ION (3 entities in total)
• Functional Keywords: cell cycle, apc10/doc1, apc/cyclosome, ubiquitination, e3 ubiquitin ligase, beta sandwich, jelly roll
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Cytoplasm : P53068
• Total number of polymer chains: 2
• Total formula weight: 51735.13

Authors

Au, S.W.N.,Leng, X.,Harper, J.W.A.D.E.,Barford, D. (deposition date: 2001-11-28, release date: 2002-03-15, Last modification date: 2024-05-08)

Primary citation

Au, S.W.N.,Leng, X.,Harper, J.W.A.D.E.,Barford, D.
Implications for the Ubiquitination Reaction of the Anaphase-Promoting Complex from the Crystal Structure of the Doc1/Apc10 Subunit.
J.Mol.Biol., 316:955-, 2002

PubMed Abstract: 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.

PubMed: 11884135
DOI: 10.1006/JMBI.2002.5399

Experimental method

X-RAY DIFFRACTION (2.2 Å)