1urh
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1urh.gif|left|200px]] | + | [[Image:1urh.gif|left|200px]] |
| - | + | ||
| - | '''THE "RHODANESE" FOLD AND CATALYTIC MECHANISM OF 3-MERCAPTOPYRUVATE SULFOTRANSFERASES: CRYSTAL STRUCTURE OF SSEA FROM ESCHERICHIA COLI''' | + | {{Structure |
| + | |PDB= 1urh |SIZE=350|CAPTION= <scene name='initialview01'>1urh</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO3:SULFITE ION'>SO3</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/3-mercaptopyruvate_sulfurtransferase 3-mercaptopyruvate sulfurtransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.1.2 2.8.1.2] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE "RHODANESE" FOLD AND CATALYTIC MECHANISM OF 3-MERCAPTOPYRUVATE SULFOTRANSFERASES: CRYSTAL STRUCTURE OF SSEA FROM ESCHERICHIA COLI''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1URH is a [ | + | 1URH 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=1URH OCA]. |
==Reference== | ==Reference== | ||
| - | The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: crystal structure of SseA from Escherichia coli., Spallarossa A, Forlani F, Carpen A, Armirotti A, Pagani S, Bolognesi M, Bordo D, J Mol Biol. 2004 Jan 9;335(2):583-93. PMID:[http:// | + | The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: crystal structure of SseA from Escherichia coli., Spallarossa A, Forlani F, Carpen A, Armirotti A, Pagani S, Bolognesi M, Bordo D, J Mol Biol. 2004 Jan 9;335(2):583-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14672665 14672665] |
[[Category: 3-mercaptopyruvate sulfurtransferase]] | [[Category: 3-mercaptopyruvate sulfurtransferase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| Line 26: | Line 35: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:35:43 2008'' |
Revision as of 12:35, 20 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | 3-mercaptopyruvate sulfurtransferase, with EC number 2.8.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE "RHODANESE" FOLD AND CATALYTIC MECHANISM OF 3-MERCAPTOPYRUVATE SULFOTRANSFERASES: CRYSTAL STRUCTURE OF SSEA FROM ESCHERICHIA COLI
Overview
3-Mercaptopyruvate sulfurtransferases (MSTs) catalyze, in vitro, the transfer of a sulfur atom from substrate to cyanide, yielding pyruvate and thiocyanate as products. They display clear structural homology with the protein fold observed in the rhodanese sulfurtransferase family, composed of two structurally related domains. The role of MSTs in vivo, as well as their detailed molecular mechanisms of action have been little investigated. Here, we report the crystal structure of SseA, a MST from Escherichia coli, which is the first MST three-dimensional structure disclosed to date. SseA displays specific structural differences relative to eukaryotic and prokaryotic rhodaneses. In particular, conformational variation of the rhodanese active site loop, hosting the family invariant catalytic Cys residue, may support a new sulfur transfer mechanism involving Cys237 as the nucleophilic species and His66, Arg102 and Asp262 as residues assisting catalysis.
About this Structure
1URH is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: crystal structure of SseA from Escherichia coli., Spallarossa A, Forlani F, Carpen A, Armirotti A, Pagani S, Bolognesi M, Bordo D, J Mol Biol. 2004 Jan 9;335(2):583-93. PMID:14672665
Page seeded by OCA on Thu Mar 20 14:35:43 2008
