2XPI
Crystal structure of APC/C hetero-tetramer Cut9-Hcn1
Summary for 2XPI
| Entry DOI | 10.2210/pdb2xpi/pdb |
| Descriptor | ANAPHASE-PROMOTING COMPLEX SUBUNIT CUT9, ANAPHASE-PROMOTING COMPLEX SUBUNIT HCN1 HCN1/CDC26,20S CYCLOSOME/APC COMPLEX PROTEIN HCN1, CHAPERONE-LIKE PROTEIN HCN1, HIGH COPY SUPPRESSOR OF CUT9 PROTEIN 1, GOLD (I) CYANIDE ION, ... (4 entities in total) |
| Functional Keywords | cell cycle, tpr, ubiquitin ligase, e3, cell division, n-acetylation |
| Biological source | SCHIZOSACCHAROMYCES POMBE More |
| Total number of polymer chains | 4 |
| Total formula weight | 154327.39 |
| Authors | Zhang, Z.,Kulkarni, K.A.,Barford, D. (deposition date: 2010-08-26, release date: 2011-03-30, Last modification date: 2024-11-06) |
| Primary citation | Zhang, Z.,Kulkarni, K.A.,Hanrahan, S.J.,Thompson, A.J.,Barford, D. The Apc/C Subunit Cdc16/Cut9 is a Contiguous Tetratricopeptide Superhelix with a Homo-Dimer Interface Similar to Cdc27 Embo J., 29:3733-, 2010 Cited by PubMed Abstract: The anaphase-promoting complex/cyclosome (APC/C), an E3 ubiquitin ligase responsible for controlling cell cycle transitions, is a multisubunit complex assembled from 13 different proteins. Numerous APC/C subunits incorporate multiple copies of the tetratricopeptide repeat (TPR). Here, we report the crystal structure of Schizosaccharomyces pombe Cut9 (Cdc16/Apc6) in complex with Hcn1 (Cdc26), showing that Cdc16/Cut9 is a contiguous TPR superhelix of 14 TPR units. A C-terminal block of TPR motifs interacts with Hcn1, whereas an N-terminal TPR block mediates Cdc16/Cut9 self-association through a homotypic interface. This dimer interface is structurally related to the N-terminal dimerization domain of Cdc27, demonstrating that both Cdc16/Cut9 and Cdc27 form homo-dimers through a conserved mechanism. The acetylated N-terminal Met residue of Hcn1 is enclosed within a chamber created from the Cut9 TPR superhelix. Thus, in complex with Cdc16/Cut9, the N-acetyl-Met residue of Hcn1, a putative degron for the Doa10 E3 ubiquitin ligase, is inaccessible for Doa10 recognition, protecting Hcn1/Cdc26 from ubiquitin-dependent degradation. This finding may provide a structural explanation for a mechanism to control the stoichiometry of proteins participating in multisubunit complexes. PubMed: 20924356DOI: 10.1038/EMBOJ.2010.247 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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