title: Mechanism for the hydrolysis of a sulfur-sulfur bond based on the crystal structure of the thiosulfohydrolase SoxB.
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.
authors.affiliation: Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
authors.forename: Véronique
authors.initials: V
authors.lastname: Sauvé
authors.forename: Pietro
authors.initials: P
authors.lastname: Roversi
authors.forename: Kirstin J
authors.initials: KJ
authors.lastname: Leath
authors.forename: Elspeth F
authors.initials: EF
authors.lastname: Garman
authors.forename: Robin
authors.initials: R
authors.lastname: Antrobus
authors.forename: Susan M
authors.initials: SM
authors.lastname: Lea
authors.forename: Ben C
authors.initials: BC
authors.lastname: Berks
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D003593:Cytoplasm / Q000378:metabolism; D005786:Gene Expression Regulation; D006868:Hydrolysis; D008956:Models, Chemical; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D011485:Protein Binding; D011994:Recombinant Proteins / Q000737:chemistry; D055748:SOXB1 Transcription Factors / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D013455:Sulfur / Q000737:chemistry; D016963:Thermus thermophilus / Q000201:enzymology*
chemical_list: D011994:Recombinant Proteins; D055748:SOXB1 Transcription Factors; D013455:Sulfur