1GHE

CRYSTAL STRUCTURE OF TABTOXIN RESISTANCE PROTEIN COMPLEXED WITH AN ACYL COENZYME A

1GHE の概要

• エントリーDOI: 10.2210/pdb1ghe/pdb
• 分子名称: ACETYLTRANSFERASE, ACETYL COENZYME *A (3 entities in total)
• 機能のキーワード: acyl coenzyme a complex, transferase
• 由来する生物種: Pseudomonas syringae pv. tabaci
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40604.03

構造登録者

He, H.,Ding, Y.,Bartlam, M.,Sun, F.,Le, Y.,Qin, X.,Tang, H.,Zhang, R.,Joachimiak, A.,Liu, Y.,Zhao, N.,Rao, Z. (登録日: 2000-12-13, 公開日: 2003-01-14, 最終更新日: 2024-11-06)

主引用文献

He, H.,Ding, Y.,Bartlam, M.,Sun, F.,Le, Y.,Qin, X.,Tang, H.,Zhang, R.,Joachimiak, A.,Liu, Y.,Zhao, N.,Rao, Z.
Crystal Structure of Tabtoxin Resistance Protein Complexed with Acetyl Coenzyme A Reveals the Mechanism for beta-Lactam Acetylation
J.Mol.Biol., 325:1019-1030, 2003

PubMed Abstract: Tabtoxin resistance protein (TTR) is an enzyme that renders tabtoxin-producing pathogens, such as Pseudomonas syringae, tolerant to their own phytotoxins. Here, we report the crystal structure of TTR complexed with its natural cofactor, acetyl coenzyme A (AcCoA), to 1.55A resolution. The binary complex forms a characteristic "V" shape for substrate binding and contains the four motifs conserved in the GCN5-related N-acetyltransferase (GNAT) superfamily, which also includes the histone acetyltransferases (HATs). A single-step mechanism is proposed to explain the function of three conserved residues, Glu92, Asp130 and Tyr141, in catalyzing the acetyl group transfer to its substrate. We also report that TTR possesses HAT activity and suggest an evolutionary relationship between TTR and other GNAT members.

PubMed: 12527305
DOI: 10.1016/S0022-2836(02)01284-6

実験手法

X-RAY DIFFRACTION (1.55 Å)