1IAX
CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH PLP
Summary for 1IAX
| Entry DOI | 10.2210/pdb1iax/pdb |
| Related | 1IAY |
| Descriptor | 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE 2, SULFATE ION, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | plp-dependent enzymes, lyase |
| Biological source | Solanum lycopersicum |
| Total number of polymer chains | 2 |
| Total formula weight | 97274.64 |
| Authors | |
| Primary citation | Huai, Q.,Xia, Y.,Chen, Y.,Callahan, B.,Li, N.,Ke, H. Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms J.Biol.Chem., 276:38210-38216, 2001 Cited by PubMed Abstract: 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. PubMed: 11431475DOI: 10.1074/jbc.M008127200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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