Ontology highlight
ABSTRACT:
SUBMITTER: Sauve V
PROVIDER: S-EPMC2755893 | biostudies-literature | 2009 Aug
REPOSITORIES: biostudies-literature
Sauvé Véronique V Roversi Pietro P Leath Kirstin J KJ Garman Elspeth F EF Antrobus Robin R Lea Susan M SM Berks Ben C BC
The Journal of biological chemistry 20090616 32
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 pr ...[more]