3zn3
From Proteopedia
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| - | {{STRUCTURE_3zn3| PDB=3zn3 | SCENE= }} | ||
| - | ===N-terminal domain of S. pombe Cdc23 APC subunit=== | ||
| - | {{ABSTRACT_PUBMED_23583778}} | ||
| - | == | + | ==N-terminal domain of S. pombe Cdc23 APC subunit== |
| - | [[http://www.uniprot.org/uniprot/APC8_SCHPO APC8_SCHPO | + | <StructureSection load='3zn3' size='340' side='right'caption='[[3zn3]], [[Resolution|resolution]] 1.90Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3zn3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZN3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZN3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zn3 OCA], [https://pdbe.org/3zn3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zn3 RCSB], [https://www.ebi.ac.uk/pdbsum/3zn3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zn3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/APC8_SCHPO APC8_SCHPO] Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Has a role in promoting metaphase to anaphase transition via the ubiquitination of specific mitotic substrates.<ref>PMID:10526233</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The anaphase-promoting complex or cyclosome (APC/C) is a large E3 RING-cullin ubiquitin ligase composed of between 14 and 15 individual proteins. A striking feature of the APC/C is that only four proteins are involved in directly recognizing target proteins and catalyzing the assembly of a polyubiquitin chain. All other subunits, which account for >80% of the mass of the APC/C, provide scaffolding functions. A major proportion of these scaffolding subunits are structurally related. In metazoans, there are four canonical tetratricopeptide repeat (TPR) proteins that form homo-dimers (Apc3/Cdc27, Apc6/Cdc16, Apc7 and Apc8/Cdc23). Here, we describe the crystal structure of the N-terminal homo-dimerization domain of Schizosaccharomyces pombe Cdc23 (Cdc23Nterm). Cdc23Nterm is composed of seven contiguous TPR motifs that self-associate through a related mechanism to those of Cdc16 and Cdc27. Using the Cdc23Nterm structure, we generated a model of full-length Cdc23. The resultant "V"-shaped molecule docks into the Cdc23-assigned density of the human APC/C structure determined using negative stain electron microscopy (EM). Based on sequence conservation, we propose that Apc7 forms a homo-dimeric structure equivalent to those of Cdc16, Cdc23 and Cdc27. The model is consistent with the Apc7-assigned density of the human APC/C EM structure. The four canonical homo-dimeric TPR proteins of human APC/C stack in parallel on one side of the complex. Remarkably, the uniform relative packing of neighboring TPR proteins generates a novel left-handed suprahelical TPR assembly. This finding has implications for understanding the assembly of other TPR-containing multimeric complexes. | ||
| - | + | The Four Canonical TPR Subunits of Human APC/C Form Related Homo-Dimeric Structures and Stack in Parallel to Form a TPR Suprahelix.,Zhang Z, Chang L, Yang J, Conin N, Kulkarni K, Barford D J Mol Biol. 2013 Apr 11. pii: S0022-2836(13)00233-7. doi:, 10.1016/j.jmb.2013.04.004. PMID:23583778<ref>PMID:23583778</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 3zn3" style="background-color:#fffaf0;"></div> |
| - | [[Category: Barford | + | == References == |
| - | [[Category: Conin | + | <references/> |
| - | [[Category: Kulkarni | + | __TOC__ |
| - | [[Category: Yang | + | </StructureSection> |
| - | [[Category: Zhang | + | [[Category: Large Structures]] |
| - | + | [[Category: Schizosaccharomyces pombe]] | |
| - | + | [[Category: Barford D]] | |
| + | [[Category: Conin N]] | ||
| + | [[Category: Kulkarni K]] | ||
| + | [[Category: Yang J]] | ||
| + | [[Category: Zhang Z]] | ||
Current revision
N-terminal domain of S. pombe Cdc23 APC subunit
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