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5BPT

Atomic-resolution structures of the APC/C subunits Apc4 and the Apc5 N-terminal domain

Summary for 5BPT
Entry DOI10.2210/pdb5bpt/pdb
DescriptorMGC81278 protein (1 entity in total)
Functional Keywordscell cycle, apc4, apc/c, anaphase promoting complex
Biological sourceXenopus laevis (African clawed frog)
Total number of polymer chains1
Total formula weight85415.21
Authors
Cronin, N.,Yang, J.,Zhang, Z.,Barford, D. (deposition date: 2015-05-28, release date: 2015-09-02, Last modification date: 2024-10-16)
Primary citationCronin, N.B.,Yang, J.,Zhang, Z.,Kulkarni, K.,Chang, L.,Yamano, H.,Barford, D.
Atomic-Resolution Structures of the APC/C Subunits Apc4 and the Apc5 N-Terminal Domain.
J.Mol.Biol., 427:3300-3315, 2015
Cited by
PubMed Abstract: Many essential biological processes are mediated by complex molecular machines comprising multiple subunits. Knowledge on the architecture of individual subunits and their positions within the overall multimeric complex is key to understanding the molecular mechanisms of macromolecular assemblies. The anaphase-promoting complex/cyclosome (APC/C) is a large multisubunit complex that regulates cell cycle progression by ubiquitinating cell cycle proteins for proteolysis by the proteasome. The holo-complex is composed of 15 different proteins that assemble to generate a complex of 20 subunits. Here, we describe the crystal structures of Apc4 and the N-terminal domain of Apc5 (Apc5(N)). Apc4 comprises a WD40 domain split by a long α-helical domain, whereas Apc5(N) has an α-helical fold. In a separate study, we had fitted these atomic models to a 3.6-Å-resolution cryo-electron microscopy map of the APC/C. We describe how, in the context of the APC/C, regions of Apc4 disordered in the crystal assume order through contacts to Apc5, whereas Apc5(N) shows small conformational changes relative to its crystal structure. We discuss the complementary approaches of high-resolution electron microscopy and protein crystallography to the structure determination of subunits of multimeric complexes.
PubMed: 26343760
DOI: 10.1016/j.jmb.2015.08.023
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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數據於2024-11-06公開中

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