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4rg7

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==Crystal structure of APC3==
==Crystal structure of APC3==
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<StructureSection load='4rg7' size='340' side='right' caption='[[4rg7]], [[Resolution|resolution]] 4.25&Aring;' scene=''>
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<StructureSection load='4rg7' size='340' side='right'caption='[[4rg7]], [[Resolution|resolution]] 4.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4rg7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RG7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RG7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4rg7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RG7 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rg6|4rg6]], [[4rg9|4rg9]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.25&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rg7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rg7 RCSB], [http://www.ebi.ac.uk/pdbsum/4rg7 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rg7 OCA], [https://pdbe.org/4rg7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rg7 RCSB], [https://www.ebi.ac.uk/pdbsum/4rg7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rg7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CDC27_HUMAN CDC27_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.<ref>PMID:18485873</ref>
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[https://www.uniprot.org/uniprot/CDC27_HUMAN CDC27_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.<ref>PMID:18485873</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Anaphase Promoting Complex/Cyclosome (APC/C) is a massive E3 ligase that controls mitosis by catalyzing ubiquitination of key cell cycle regulatory proteins. The APC/C assembly contains two subcomplexes: the "Platform" centers around a cullin-RING-like E3 ligase catalytic core; the "Arc Lamp" is a hub that mediates transient association with regulators and ubiquitination substrates. The Arc Lamp contains the small subunits APC16, CDC26, and APC13, and tetratricopeptide repeat (TPR) proteins (APC7, APC3, APC6, and APC8) that homodimerize and stack with quasi-twofold symmetry. Within the APC/C complex, APC3 serves as center for regulation. APC3's TPR motifs recruit substrate-binding coactivators, CDC20 and CDH1, via their C-terminal conserved Ile-Arg (IR) tail sequences. Human APC3 also binds APC16 and APC7, and contains a &gt;200-residue loop that is heavily phosphorylated during mitosis, although the basis for APC3 interactions and whether loop phosphorylation is required for ubiquitination are unclear. Here, we map the basis for human APC3 assembly with APC16 and APC7, report crystal structures of APC3Deltaloop alone and in complex with the C-terminal domain of APC16, and test roles of APC3's loop and IR-tail binding surfaces in APC/C-catalyzed ubiquitination. The structures show how one APC16 binds asymmetrically to the symmetric APC3 dimer, and together with biochemistry and prior data explain how APC16 recruits APC7 to APC3, show how APC3's C-terminal domain is rearranged in the full APC/C assembly, and visualize residues in the IR-tail binding cleft important for coactivator-dependent ubiquitination. Overall, the results provide insights into assembly, regulation, and interactions of TPR proteins and the APC/C.
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Structure of an APC3-APC16 complex: Insights into assembly of the Anaphase Promoting Complex/Cyclosome.,Yamaguchi M, Yu S, Qiao R, Weissmann F, Miller DJ, VanderLinden R, Brown NG, Frye JJ, Peters JM, Schulman BA J Mol Biol. 2014 Dec 6. pii: S0022-2836(14)00616-0. doi:, 10.1016/j.jmb.2014.11.020. PMID:25490258<ref>PMID:25490258</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Miller, D J]]
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[[Category: Homo sapiens]]
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[[Category: Schulman, B A]]
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[[Category: Large Structures]]
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[[Category: Yamaguchi, M]]
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[[Category: Miller DJ]]
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[[Category: Yu, S]]
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[[Category: Schulman BA]]
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[[Category: Protein assembly]]
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[[Category: Yamaguchi M]]
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[[Category: Protein binding]]
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[[Category: Yu S]]
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[[Category: Symmetric homodimer]]
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[[Category: Tpr fplding]]
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Current revision

Crystal structure of APC3

PDB ID 4rg7

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