5bpw | pdb_00005bpw

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

spinqualitylabelsall models 5bpw, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5bpw is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function APC4_HUMAN Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Publication Abstract from PubMed 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 alpha-helical domain, whereas Apc5(N) has an alpha-helical fold. In a separate study, we had fitted these atomic models to a 3.6-A-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. Atomic-Resolution Structures of the APC/C Subunits Apc4 and the Apc5 N-Terminal Domain.,Cronin NB, Yang J, Zhang Z, Kulkarni K, Chang L, Yamano H, Barford D J Mol Biol. 2015 Oct 9;427(20):3300-15. doi: 10.1016/j.jmb.2015.08.023. Epub 2015, Sep 4. PMID:26343760 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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