1IAY

CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH COFACTOR PLP AND INHIBITOR AVG

1IAY の概要

• エントリーDOI: 10.2210/pdb1iay/pdb
• 関連するPDBエントリー: 1IAX
• 分子名称: 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE 2, PYRIDOXAL-5'-PHOSPHATE, 2-AMINO-4-(2-AMINO-ETHOXY)-BUTYRIC ACID, ... (4 entities in total)
• 機能のキーワード: protein-cofactor-inhibitor complex, v6-dependent enzyme, lyase
• 由来する生物種: Solanum lycopersicum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48703.44

構造登録者

Huai, Q.,Xia, Y.,Chen, Y.,Callahan, B.,Li, N.,Ke, H. (登録日: 2001-03-24, 公開日: 2001-04-04, 最終更新日: 2025-03-26)

主引用文献

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

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: 11431475
DOI: 10.1074/jbc.M008127200

実験手法

X-RAY DIFFRACTION (2.7 Å)