1JED

Crystal Structure of ATP Sulfurylase in complex with ADP

Summary for 1JED

• Entry DOI: 10.2210/pdb1jed/pdb
• Related: 1G8F 1G8G 1G8H 1JEC 1JEE
• Descriptor: SULFATE ADENYLYLTRANSFERASE, CADMIUM ION, CALCIUM ION, ... (9 entities in total)
• Functional Keywords: alpha-beta protein, beta-barrel, rossmann-fold, inhibitor complex, adp, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P08536
• Total number of polymer chains: 2
• Total formula weight: 119171.64

Authors

Ullrich, T.C.,Huber, R. (deposition date: 2001-06-17, release date: 2001-11-14, Last modification date: 2023-08-16)

Primary citation

Ullrich, T.C.,Huber, R.
The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle.
J.Mol.Biol., 313:1117-1125, 2001

PubMed Abstract: 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.

PubMed: 11700067
DOI: 10.1006/jmbi.2001.5098

Experimental method

X-RAY DIFFRACTION (2.95 Å)