1SUR

PHOSPHO-ADENYLYL-SULFATE REDUCTASE

Summary for 1SUR

• Entry DOI: 10.2210/pdb1sur/pdb
• Descriptor: PAPS REDUCTASE (1 entity in total)
• Functional Keywords: assimilatory sulfate reduction, 3-phospho-adenylyl-sulfate reductase, oxidoreductase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P17854
• Total number of polymer chains: 1
• Total formula weight: 24595.89

Authors

Sinning, I.,Savage, H. (deposition date: 1998-04-01, release date: 1999-05-11, Last modification date: 2024-02-14)

Primary citation

Savage, H.,Montoya, G.,Svensson, C.,Schwenn, J.D.,Sinning, I.
Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases.
Structure, 5:895-906, 1997

PubMed Abstract: Assimilatory sulphate reduction supplies prototrophic organisms with reduced sulphur for the biosynthesis of all sulphur-containing metabolites. This process is driven by a sequence of enzymatic steps involving phosphoadenylyl sulphate (PAPS) reductase. Thioredoxin is used as the electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP) and sulphite. Unlike most electron-transfer reactions, there are no cofactors or prosthetic groups involved in this reduction and PAPS reductase is one of the rare examples of an enzyme that is able to store two electrons. Determination of the structure of PAPS reductase is the first step towards elucidating the biochemical details of the reduction of PAPS to sulphite.

PubMed: 9261082
DOI: 10.1016/S0969-2126(97)00244-X

Experimental method

X-RAY DIFFRACTION (2 Å)