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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
32
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pubmed:dateCreated |
2009-8-3
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21707-18
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pubmed:dateRevised |
2010-9-24
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pubmed:meshHeading |
pubmed-meshheading:19535341-Amino Acid Sequence,
pubmed-meshheading:19535341-Crystallography, X-Ray,
pubmed-meshheading:19535341-Cytoplasm,
pubmed-meshheading:19535341-Gene Expression Regulation,
pubmed-meshheading:19535341-Hydrolysis,
pubmed-meshheading:19535341-Models, Chemical,
pubmed-meshheading:19535341-Molecular Conformation,
pubmed-meshheading:19535341-Molecular Sequence Data,
pubmed-meshheading:19535341-Protein Binding,
pubmed-meshheading:19535341-Recombinant Proteins,
pubmed-meshheading:19535341-SOXB1 Transcription Factors,
pubmed-meshheading:19535341-Sequence Homology, Amino Acid,
pubmed-meshheading:19535341-Substrate Specificity,
pubmed-meshheading:19535341-Sulfur,
pubmed-meshheading:19535341-Thermus thermophilus
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pubmed:year |
2009
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pubmed:articleTitle |
Mechanism for the hydrolysis of a sulfur-sulfur bond based on the crystal structure of the thiosulfohydrolase SoxB.
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pubmed:affiliation |
Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
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