2jts
From Proteopedia
(New page: '''Unreleased structure''' The entry 2jts is ON HOLD until Paper Publication Authors: Jin, C., Li, H. Description: rhodanese with anions from E. coli ''Page seeded by [http://oca.weizm...) |
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| + | {{STRUCTURE_2jts| PDB=2jts | SCENE= }} | ||
| - | + | '''rhodanese with anions from E. coli''' | |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun | + | ==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. | ||
| + | |||
| + | ==About this Structure== | ||
| + | 2JTS 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=2JTS OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18355042 18355042] | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Single protein]] | ||
| + | [[Category: Jin, C.]] | ||
| + | [[Category: Li, H.]] | ||
| + | [[Category: Solution structure rhodanese anion]] | ||
| + | [[Category: Stress response]] | ||
| + | [[Category: Transferase]] | ||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:02:15 2008'' | ||
Revision as of 09:02, 18 June 2008
rhodanese with anions 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.
About this Structure
2JTS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Wed Jun 18 12:02:15 2008
