2mrm
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Solution structure of the rhodanese domain of YgaP from E. coli== |
| + | <StructureSection load='2mrm' size='340' side='right' caption='[[2mrm]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mrm]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MRM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MRM FirstGlance]. <br> | ||
| + | </td></tr><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=2mrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mrm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mrm RCSB], [http://www.ebi.ac.uk/pdbsum/2mrm PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rhodanese domains are abundant structural modules that catalyze the transfer of a sulfur atom from thiolsulfates to cyanide via formation of a covalent persulfide intermediate that is bound to an essential conserved cysteine residue. In this study, the three-dimensional structure of the rhodanese domain of YgaP from Escherichia coli was determined using solution NMR. A typical rhodanese domain fold was observed, as expected from the high homology with the catalytic domain of other sulfur transferases. The initial sulfur-transfer step and formation of the rhodanese persulfide intermediate were monitored by addition of sodium thiosulfate using two-dimensional (1)H-(15)N correlation spectroscopy. Discrete sharp signals were observed upon substrate addition, indicting fast exchange between sulfur-free and persulfide-intermediate forms. Residues exhibiting pronounced chemical shift changes were mapped to the structure, and included both substrate binding and surrounding residues. | ||
| - | + | Fast conformational exchange between the sulfur-free and persulfide-bound rhodanese domain of E. coli YgaP.,Wang W, Zhou P, He Y, Yu L, Xiong Y, Tian C, Wu F Biochem Biophys Res Commun. 2014 Sep 26;452(3):817-21. doi:, 10.1016/j.bbrc.2014.09.002. Epub 2014 Sep 7. PMID:25204500<ref>PMID:25204500</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Tian, C.]] | ||
| + | [[Category: Wang, W.]] | ||
| + | [[Category: Wu, F.]] | ||
| + | [[Category: Zhou, P.]] | ||
| + | [[Category: E. coli]] | ||
| + | [[Category: Integral membrane protein]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Rhodanese domain]] | ||
| + | [[Category: Ygap]] | ||
Revision as of 07:34, 8 October 2014
Solution structure of the rhodanese domain of YgaP from E. coli
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