Structural highlights
Function
[MET3_PENCH] Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of the cooperative hexameric enzyme ATP sulfurylase from Penicillium chrysogenum bound to its allosteric inhibitor, 3'-phosphoadenosine-5'-phosphosulfate (PAPS), was determined to 2.6 A resolution. This structure represents the low substrate-affinity T-state conformation of the enzyme. Comparison with the high substrate-affinity R-state structure reveals that a large rotational rearrangement of domains occurs as a result of the R-to-T transition. The rearrangement is accompanied by the 17 A movement of a 10-residue loop out of the active site region, resulting in an open, product release-like structure of the catalytic domain. Binding of PAPS is proposed to induce the allosteric transition by destabilizing an R-state-specific salt linkage between Asp 111 in an N-terminal domain of one subunit and Arg 515 in the allosteric domain of a trans-triad subunit. Disrupting this salt linkage by site-directed mutagenesis induces cooperative inhibition behavior in the absence of an allosteric effector, confirming the role of these two residues.
Allosteric inhibition via R-state destabilization in ATP sulfurylase from Penicillium chrysogenum.,MacRae IJ, Segel IH, Fisher AJ Nat Struct Biol. 2002 Dec;9(12):945-9. PMID:12426581[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ MacRae IJ, Segel IH, Fisher AJ. Allosteric inhibition via R-state destabilization in ATP sulfurylase from Penicillium chrysogenum. Nat Struct Biol. 2002 Dec;9(12):945-9. PMID:12426581 doi:10.1038/nsb868
