2jtr: Difference between revisions

Revision as of 13:58, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2jtr.png

Template:STRUCTURE 2jtr

rhodanese persulfide from E. colirhodanese persulfide from E. coli

Template:ABSTRACT PUBMED 18355042

About this StructureAbout this Structure

2JTR is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

ReferenceReference

Solution structures and backbone dynamics of Escherichia coli rhodanese PspE in its sulfur-free and persulfide-intermediate forms: implications for the catalytic mechanism of rhodanese., Li H, Yang F, Kang X, Xia B, Jin C, Biochemistry. 2008 Apr 15;47(15):4377-85. Epub 2008 Mar 21. PMID:18355042

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OCA

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-'''rhodanese persulfide from E. coli'''
+===rhodanese persulfide from E. coli===
-==Overview==
+<!--
-Rhodanese catalyzes the sulfur-transfer reaction that transfers sulfur from thiosulfate to cyanide by a double-displacement mechanism, in which an active cysteine residue plays a central role. Previous studies indicated that the phage-shock protein E (PspE) from Escherichia coli is a rhodanese composed of a single active domain and is the only accessible rhodanese among the three single-domain rhodaneses in E. coli. To understand the catalytic mechanism of rhodanese at the molecular level, we determined the solution structures of the sulfur-free and persulfide-intermediate forms of PspE by nuclear magnetic resonance (NMR) spectroscopy and identified the active site by NMR titration experiments. To obtain further insights into the catalytic mechanism, we studied backbone dynamics by NMR relaxation experiments. Our results demonstrated that the overall structures in both sulfur-free and persulfide-intermediate forms are highly similar, suggesting that no significant conformational changes occurred during the catalytic reaction. However, the backbone dynamics revealed that the motional properties of PspE in its sulfur-free form are different from the persulfide-intermediate state. The conformational exchanges are largely enhanced in the persulfide-intermediate form of PspE, especially around the active site. The present structural and biochemical studies in combination with backbone dynamics provide further insights in understanding the catalytic mechanism of rhodanese.
+The line below this paragraph, {{ABSTRACT_PUBMED_18355042}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18355042 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18355042}}
 ==About this Structure==
-JTR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JTR OCA].
+JTR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JTR OCA].
 ==Reference==
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 [[Category: Stress response]]
 [[Category: Transferase]]
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