1jed
Crystal Structure of ATP Sulfurylase in complex with ADP
|
OverviewOverview
The ubiquitous enzyme ATP sulfurylase (ATPS) catalyzes the primary step of, intracellular sulfate activation, the formation of adenosine, 5'-phosphosulfate (APS). It has been shown that the enzyme catalyzes the, generation of APS from ATP and inorganic sulfate in vitro and in vivo, and, that this reaction can be inhibited by a number of simple molecules. Here, we present the crystal structures of ATPS from the yeast Saccharomyces, cerevisiae complexed with compounds that have inhibitory effects on the, catalytic reaction of ATPS. Thiosulfate and ADP mimic the substrates, sulfate and ATP in the active site, but are non-reactive and thus, competitive inhibitors of the sulfurylase reaction. Chlorate is bound in a, crevice between the active site and the intermediate domain III of the, complex structure. It forms hydrogen bonds to residues of both domains and, stabilizes a "closed" conformation, inhibiting the release of the reaction, products APS and PPi. These new observations are evidence for the crucial, role of the displacement mechanism for the catalysis by ATPS.
About this StructureAbout this Structure
1JED is a Single protein structure of sequence from Saccharomyces cerevisiae with CD, CA, NA, MG, ADP, TRS and ACY as ligands. Active as Sulfate adenylyltransferase, with EC number 2.7.7.4 Full crystallographic information is available from OCA.
ReferenceReference
The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle., Ullrich TC, Huber R, J Mol Biol. 2001 Nov 9;313(5):1117-25. PMID:11700067
Page seeded by OCA on Tue Nov 20 18:09:46 2007