3zn3

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{{STRUCTURE_3zn3| PDB=3zn3 | SCENE= }}
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==N-terminal domain of S. pombe Cdc23 APC subunit==
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===N-terminal domain of S. pombe Cdc23 APC subunit===
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<StructureSection load='3zn3' size='340' side='right' caption='[[3zn3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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{{ABSTRACT_PUBMED_23583778}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3zn3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZN3 FirstGlance]. <br>
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==Function==
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></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=3zn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zn3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zn3 RCSB], [http://www.ebi.ac.uk/pdbsum/3zn3 PDBsum]</span></td></tr>
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</table>
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== Function ==
[[http://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>
[[http://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>
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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 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 &gt;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.
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==About this Structure==
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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>
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[[3zn3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZN3 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:023583778</ref><references group="xtra"/><references/>
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</div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Cbs 356]]
[[Category: Cbs 356]]
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[[Category: Barford, D.]]
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[[Category: Barford, D]]
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[[Category: Conin, N.]]
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[[Category: Conin, N]]
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[[Category: Kulkarni, K.]]
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[[Category: Kulkarni, K]]
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[[Category: Yang, J.]]
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[[Category: Yang, J]]
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[[Category: Zhang, Z.]]
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[[Category: Zhang, Z]]
[[Category: Cell cycle]]
[[Category: Cell cycle]]
[[Category: Tpr]]
[[Category: Tpr]]

Revision as of 21:25, 24 December 2014

N-terminal domain of S. pombe Cdc23 APC subunit

3zn3, resolution 1.90Å

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