1JHJ

Crystal structure of the APC10/Doc1 subunit of the human anaphase-promoting complex

Summary for 1JHJ

• Entry DOI: 10.2210/pdb1jhj/pdb
• Descriptor: APC10, NICKEL (II) ION (3 entities in total)
• Functional Keywords: beta sandwich, jellyroll, cell cycle
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 19558.65

Authors

Wendt, K.S.,Vodermaier, H.C.,Jacob, U.,Gieffers, C.,Gmachl, M.,Peters, J.-M.,Huber, R.,Sondermann, P. (deposition date: 2001-06-28, release date: 2001-10-24, Last modification date: 2024-05-29)

Primary citation

Wendt, K.S.,Vodermaier, H.C.,Jacob, U.,Gieffers, C.,Gmachl, M.,Peters, J.M.,Huber, R.,Sondermann, P.
Crystal structure of the APC10/DOC1 subunit of the human anaphase-promoting complex
Nat.Struct.Biol., 8:784-788, 2001

PubMed Abstract: The anaphase-promoting complex (APC), or cyclosome, is a cell cycle-regulated ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC is composed of at least 11 subunits; no structure has been determined for any of these subunits. The subunit APC10/DOC1, a one-domain protein consisting of 185 amino acids, has a conserved core (residues 22-161) that is homologous to domains found in several other putative ubiquitin ligases and, therefore, may play a role in ubiquitination reactions. Here we report the crystal structure of human APC10 at 1.6 A resolution. The core of the protein is formed by a beta-sandwich that adopts a jellyroll fold. Unexpectedly, this structure is highly similar to ligand-binding domains of several bacterial and eukaryotic proteins, such as galactose oxidase and coagulation factor Va, raising the possibility that APC10 may function by binding a yet unidentified ligand. We further provide biochemical evidence that the C-terminus of APC10 binds to CDC27/APC3, an APC subunit that contains multiple tetratrico peptide repeats.

PubMed: 11524682
DOI: 10.1038/nsb0901-784

Experimental method

X-RAY DIFFRACTION (1.6 Å)