Literature DB >> 19535341

Mechanism for the hydrolysis of a sulfur-sulfur bond based on the crystal structure of the thiosulfohydrolase SoxB.

Véronique Sauvé1, Pietro Roversi, Kirstin J Leath, Elspeth F Garman, Robin Antrobus, Susan M Lea, Ben C Berks.   

Abstract

SoxB is an essential component of the bacterial Sox sulfur oxidation pathway. SoxB contains a di-manganese(II) site and is proposed to catalyze the release of sulfate from a protein-bound cysteine S-thiosulfonate. A direct assay for SoxB activity is described. The structure of recombinant Thermus thermophilus SoxB was determined by x-ray crystallography to a resolution of 1.5 A. Structures were also determined for SoxB in complex with the substrate analogue thiosulfate and in complex with the product sulfate. A mechanistic model for SoxB is proposed based on these structures.

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Year:  2009        PMID： 19535341      PMCID： PMC2755893          DOI： 10.1074/jbc.M109.002709

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


  49 in total

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