1iay
CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH COFACTOR PLP AND INHIBITOR AVG
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OverviewOverview
The structures of tomato 1-aminocyclopropane-1-carboxylate synthase (ACS), in complex with either cofactor pyridoxal-5'-phosphate (PLP) or both PLP, and inhibitor aminoethoxyvinylglycine have been determined by x-ray, crystallography. The structures showed good conservation of the catalytic, residues, suggesting a similar catalytic mechanism for ACS and other, PLP-dependent enzymes. However, the proximity of Tyr152 to the C-gamma-S, bond of model substrate S-adenosylmethionine implies its critical role in, the catalysis. The concerted accomplishment of catalysis by cofactor PLP, and a protein residue, as proposed on the basis of the ACS structures in, this paper, may represent a general scheme for the diversity of, PLP-dependent catalyses. PLP-dependent enzymes have been categorized into, four types of folds. A structural comparison revealed that a core fragment, of ACS in fold type I is superimposable over tryptophan synthase beta, subunit in fold type II and mouse ornithine decarboxylase in fold type, III, thus suggesting a divergent evolution of PLP-dependent enzymes.
About this StructureAbout this Structure
1IAY is a Single protein structure of sequence from Solanum lycopersicum with PLP and AVG as ligands. Active as 1-aminocyclopropane-1-carboxylate synthase, with EC number 4.4.1.14 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms., Huai Q, Xia Y, Chen Y, Callahan B, Li N, Ke H, J Biol Chem. 2001 Oct 12;276(41):38210-6. Epub 2001 Jun 28. PMID:11431475
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