2WDC

Termus thermophilus Sulfate thiohydrolase SoxB in complex with glycerol

Summary for 2WDC

• Entry DOI: 10.2210/pdb2wdc/pdb
• Related: 2WDD 2WDE 2WDF
• Descriptor: SULFUR OXIDATION PROTEIN SOXB, GLYCEROL, ACETATE ION, ... (6 entities in total)
• Functional Keywords: sulfur-sulfur hydrolysis, sulfur oxidation pathway, sox, soxb, cys s-thiosulfonate, hydrolase
• Biological source: THERMUS THERMOPHILUS
• Total number of polymer chains: 1
• Total formula weight: 63998.69

Authors

Sauve, V.,Roversi, P.,Leath, K.J.,Garman, E.F.,Antrobus, R.,Lea, S.M.,Berks, B.C. (deposition date: 2009-03-24, release date: 2009-06-16, Last modification date: 2024-05-08)

Primary citation

Sauve, V.,Roversi, P.,Leath, K.J.,Garman, E.F.,Antrobus, R.,Lea, S.M.,Berks, B.C.
Mechanism for the Hydrolysis of a Sulfur-Sulfur Bond Based on the Crystal Structure of the Thiosulfohydrolase Soxb.
J.Biol.Chem., 284:21707-, 2009

PubMed 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.

PubMed: 19535341
DOI: 10.1074/JBC.M109.002709

Experimental method

X-RAY DIFFRACTION (1.5 Å)