2mrm: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==Solution structure of the rhodanese domain of YgaP from E. coli==

== 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>

== 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.

~~The entry 2mrm is ON HOLD until Paper Publication~~

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>

~~Authors: Wang~~, W.~~, Zhou, P~~., Tian, C., Wu, F.

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~Description~~: ~~Solution structure of the rhodanese domain of YgaP from~~ E. coli

== 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]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==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.
-The entry 2mrm is ON HOLD  until Paper Publication
+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>
-Authors: Wang, W., Zhou, P., Tian, C., Wu, F.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Solution structure of the rhodanese domain of YgaP from E. coli
+== 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]]