3kae

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Current revision (08:45, 7 February 2024) (edit) (undo)
 
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<StructureSection load='3kae' size='340' side='right'caption='[[3kae]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3kae' size='340' side='right'caption='[[3kae]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3kae]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Enccn Enccn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KAE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3kae]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Encephalitozoon_cuniculi Encephalitozoon cuniculi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KAE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.298&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NC_003237 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6035 ENCCN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3kae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kae OCA], [https://pdbe.org/3kae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kae RCSB], [https://www.ebi.ac.uk/pdbsum/3kae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kae ProSAT]</span></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=3kae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kae OCA], [https://pdbe.org/3kae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kae RCSB], [https://www.ebi.ac.uk/pdbsum/3kae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kae ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8SQV4_ENCCU Q8SQV4_ENCCU]
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The anaphase promoting complex/cyclosome (APC/C) is a large multi-subunit E3 ubiquitin ligase that targets specific cell cycle regulatory proteins for ubiquitin-dependent degradation, thereby controlling cell cycle events such as the metaphase to anaphase transition and the exit from mitosis. Biochemical and genetic studies are consistent with the notion that subunits of APC/C are organised into two distinct sub-complexes; a catalytic sub-complex including the cullin domain and RING finger subunits Apc2 and Apc11, respectively, and a tetratricopeptide repeat (TPR) sub-complex composed of the TPR subunits Cdc16, Cdc23 and Cdc27 (Apc3). Here, we describe the crystal structure of the N-terminal domain of Encephalitozoon cuniculi Cdc27 (Cdc27(Nterm)), revealing a homo-dimeric structure, composed predominantly of successive TPR motifs. Mutation of the Cdc27(Nterm) dimer interface destabilises the protein, disrupts dimerisation in solution, and abolishes the capacity of E. cuniculi Cdc27 to complement Saccharomyces cerevisiae Cdc27 in vivo. These results establish the existence of functional APC/C genes in E. cuniculi, the evolutionarily conserved dimeric properties of Cdc27, and provide a framework for understanding the architecture of full-length Cdc27.
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Molecular structure of the N-terminal domain of the APC/C subunit Cdc27 reveals a homo-dimeric tetratricopeptide repeat architecture.,Zhang Z, Roe SM, Diogon M, Kong E, El Alaoui H, Barford D J Mol Biol. 2010 Apr 16;397(5):1316-28. Epub 2010 Mar 3. PMID:20206185<ref>PMID:20206185</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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<div class="pdbe-citations 3kae" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Enccn]]
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[[Category: Encephalitozoon cuniculi]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Barford, D]]
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[[Category: Barford D]]
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[[Category: Roe, S M]]
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[[Category: Roe SM]]
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[[Category: Zhang, Z]]
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[[Category: Zhang Z]]
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[[Category: Protein binding]]
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[[Category: Tetratricopeptide repeat protein]]
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Current revision

Cdc27 N-terminus

PDB ID 3kae

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