Mechanism for the hydrolysis of a sulfur-sulfur bond based on the crystal structure of the thiosulfohydrolase SoxB.
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.
Sauvé
Véronique
V
Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
Roversi
Pietro
P
Leath
Kirstin J
KJ
Garman
Elspeth F
EF
Antrobus
Robin
R
Lea
Susan M
SM
Berks
Ben C
BC
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*
D011994:Recombinant Proteins; D055748:SOXB1 Transcription Factors; D013455:Sulfur