3zik: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3zik]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Eremothecium_gossypii Eremothecium gossypii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZIK FirstGlance]. <br> | <table><tr><td colspan='2'>[[3zik]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Eremothecium_gossypii Eremothecium gossypii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZIK FirstGlance]. <br> | ||
</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=3zik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zik OCA], [https://pdbe.org/3zik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zik RCSB], [https://www.ebi.ac.uk/pdbsum/3zik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zik ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14Å</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=3zik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zik OCA], [https://pdbe.org/3zik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zik RCSB], [https://www.ebi.ac.uk/pdbsum/3zik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zik ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q75E93_ASHGO Q75E93_ASHGO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Eremothecium gossypii]] | [[Category: Eremothecium gossypii]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chatterjee | [[Category: Chatterjee A]] | ||
[[Category: Hu | [[Category: Hu X-W]] | ||
[[Category: Singleton | [[Category: Singleton MR]] | ||
[[Category: Zakian | [[Category: Zakian S]] | ||
Latest revision as of 13:40, 9 May 2024
Structure of the Wpl1 proteinStructure of the Wpl1 protein
Structural highlights
FunctionPublication Abstract from PubMedCorrect segregation of duplicated chromosomes to daughter cells during mitosis requires the action of the cohesin complex. This tripartite ring-shaped molecule is involved in holding replicated sister chromatids together from S phase until anaphase onset. Establishment of stable cohesion involves acetylation of the Smc3 component of cohesin during replication by the Eco1 acetyltransferase. This has been proposed to antagonise the activity of another member of the cohesin complex, Wpl1. Here, we describe the X-ray structure of the conserved Wapl domain, and demonstrate that it binds the ATPase head of the Smc3 protein. We present data that suggest that Wpl1 may be involved in regulating the ATPase activity of cohesin, and that this may be subject to the acetylation state of Smc3. In addition, we present a structure of the Wapl domain bound to a functionally relevant segment of the Smc3 ATPase. Structural insights into the regulation of cohesion establishment by Wpl1.,Chatterjee A, Zakian S, Hu XW, Singleton MR EMBO J. 2013 Feb 8. doi: 10.1038/emboj.2013.16. PMID:23395900[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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