1urh
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THE "RHODANESE" FOLD AND CATALYTIC MECHANISM OF 3-MERCAPTOPYRUVATE SULFOTRANSFERASES: CRYSTAL STRUCTURE OF SSEA FROM ESCHERICHIA COLI
OverviewOverview
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 StructureAbout this Structure
1URH is a Single protein structure of sequence from Escherichia coli with SO3 as ligand. Active as 3-mercaptopyruvate sulfurtransferase, with EC number 2.8.1.2 Full crystallographic information is available from OCA.
ReferenceReference
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
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