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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.

Original publication

DOI

10.1074/jbc.M109.002709

Type

Journal article

Journal

J Biol Chem

Publication Date

07/08/2009

Volume

284

Pages

21707 - 21718

Keywords

Amino Acid Sequence, Crystallography, X-Ray, Cytoplasm, Gene Expression Regulation, Hydrolysis, Models, Chemical, Molecular Conformation, Molecular Sequence Data, Protein Binding, Recombinant Proteins, SOXB1 Transcription Factors, Sequence Homology, Amino Acid, Substrate Specificity, Sulfur, Thermus thermophilus