5n1w
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5n1w is ON HOLD until Paper Publication Authors: Chao, W.C.H., Wade, B.O., Singleton, M.R. Description: Structure of xEco2 acetyltransferase domain...) |
|||
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure of xEco2 acetyltransferase domain bound to K105-CoA conjugate== | |
| + | <StructureSection load='5n1w' size='340' side='right'caption='[[5n1w]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5n1w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N1W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N1W 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]] 2.3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8HB:(2~{S})-2-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-AMINOPURIN-9-YL)-4-OXIDANYL-3-PHOSPHONOOXY-OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]OXY-OXIDANYL-PHOSPHORYL]OXY-3,3-DIMETHYL-2-OXIDANYL-BUTANOYL]AMINO]PROPANOYLAMINO]ETHYLSULFANYL]PROPANOIC+ACID'>8HB</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5n1w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n1w OCA], [https://pdbe.org/5n1w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n1w RCSB], [https://www.ebi.ac.uk/pdbsum/5n1w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n1w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A8QZK6_XENLA A8QZK6_XENLA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sister-chromatid cohesion is established by Eco1-mediated acetylation on two conserved tandem lysines in the cohesin Smc3 subunit. However, the molecular basis of Eco1 substrate recognition and acetylation in cohesion is not fully understood. Here, we discover and rationalize the substrate specificity of Eco1 using mass spectrometry coupled with in-vitro acetylation assays and crystallography. Our structures of the X. laevis Eco2 (xEco2) bound to its primary and secondary Smc3 substrates demonstrate the plasticity of the substrate-binding site, which confers substrate specificity by concerted conformational changes of the central beta hairpin and the C-terminal extension. | ||
| - | + | Structural Basis of Eco1-Mediated Cohesin Acetylation.,Chao WC, Wade BO, Bouchoux C, Jones AW, Purkiss AG, Federico S, O'Reilly N, Snijders AP, Uhlmann F, Singleton MR Sci Rep. 2017 Mar 14;7:44313. doi: 10.1038/srep44313. PMID:28290497<ref>PMID:28290497</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5n1w" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Singleton | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Xenopus laevis]] | ||
| + | [[Category: Chao WCH]] | ||
| + | [[Category: Singleton MR]] | ||
| + | [[Category: Wade BO]] | ||
Current revision
Structure of xEco2 acetyltransferase domain bound to K105-CoA conjugate
| |||||||||||
