2mrm

</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=2mrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mrm OCA], [https://pdbe.org/2mrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mrm RCSB], [https://www.ebi.ac.uk/pdbsum/2mrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mrm ProSAT]</span></td></tr>

<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2mrm" style="background-color:#fffaf0;"></div>

== References ==

<references/>