Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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