2YKV

Structural Determinants of the Beta-Selectivity of a Bacterial Aminotransferase

2YKV の概要

• エントリーDOI: 10.2210/pdb2ykv/pdb
• 関連するPDBエントリー: 2YKU 2YKX 2YKY 4AO4
• 分子名称: BETA-TRANSAMINASE, 4'-DEOXY-4'-ACETYLYAMINO-PYRIDOXAL-5'-PHOSPHATE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: MESORHIZOBIUM SP. LUK
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 150986.36

構造登録者

Wybenga, G.G.,Crismaru, C.G.,Janssen, D.B.,Dijkstra, B.W. (登録日: 2011-05-30, 公開日: 2012-05-30, 最終更新日: 2024-05-01)

主引用文献

Wybenga, G.G.,Crismaru, C.G.,Janssen, D.B.,Dijkstra, B.W.
Structural Determinants of the Beta-Selectivity of a Bacterial Aminotransferase.
J.Biol.Chem., 287:28495-, 2012

PubMed Abstract: Chiral β-amino acids occur as constituents of various natural and synthetic compounds with potentially useful bioactivities. The pyridoxal 5'-phosphate (PLP)-dependent S-selective transaminase from Mesorhizobium sp. strain LUK (MesAT) is a fold type I aminotransferase that can be used for the preparation of enantiopure β-Phe and derivatives thereof. Using x-ray crystallography, we solved structures of MesAT in complex with (S)-β-Phe, (R)-3-amino-5-methylhexanoic acid, 2-oxoglutarate, and the inhibitor 2-aminooxyacetic acid, which allowed us to unveil the molecular basis of the amino acid specificity and enantioselectivity of this enzyme. The binding pocket of the side chain of a β-amino acid is located on the 3'-oxygen side of the PLP cofactor. The same binding pocket is utilized by MesAT to bind the α-carboxylate group of an α-amino acid. A β-amino acid thus binds in a reverse orientation in the active site of MesAT compared with an α-amino acid. Such a binding mode has not been reported before for any PLP-dependent aminotransferase and shows that the active site of MesAT has specifically evolved to accommodate both β- and α-amino acids.

PubMed: 22745123
DOI: 10.1074/JBC.M112.375238

実験手法

X-RAY DIFFRACTION (1.9 Å)