4B98

The structure of the omega aminotransferase from Pseudomonas aeruginosa

4B98 の概要

• エントリーDOI: 10.2210/pdb4b98/pdb
• 関連するPDBエントリー: 4B9B
• 分子名称: BETA-ALANINE--PYRUVATE TRANSAMINASE, 3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC ACID, PYRIDOXAL-5'-PHOSPHATE, ... (6 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: PSEUDOMONAS AERUGINOSA
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 196415.20

構造登録者

Sayer, C.,Isupov, M.N.,Westlake, A.,Littlechild, J.A. (登録日: 2012-09-03, 公開日: 2013-03-27, 最終更新日: 2023-12-20)

主引用文献

Sayer, C.,Isupov, M.N.,Westlake, A.,Littlechild, J.A.
Structural Studies with Pseudomonas and Chromobacterium [Omega]-Aminotransferases Provide Insights Into Their Differing Substrate Specificity.
Acta Crystallogr.,Sect.D, 69:564-, 2013

PubMed Abstract: The crystal structures and inhibitor complexes of two industrially important ω-aminotransferase enzymes from Pseudomonas aeruginosa and Chromobacterium violaceum have been determined in order to understand the differences in their substrate specificity. The two enzymes share 30% sequence identity and use the same amino acceptor, pyruvate; however, the Pseudomonas enzyme shows activity towards the amino donor β-alanine, whilst the Chromobacterium enzyme does not. Both enzymes show activity towards S-α-methylbenzylamine (MBA), with the Chromobacterium enzyme having a broader substrate range. The crystal structure of the P. aeruginosa enzyme has been solved in the holo form and with the inhibitor gabaculine bound. The C. violaceum enzyme has been solved in the apo and holo forms and with gabaculine bound. The structures of the holo forms of both enzymes are quite similar. There is little conformational difference observed between the inhibitor complex and the holoenzyme for the P. aeruginosa aminotransferase. In comparison, the crystal structure of the C. violaceum gabaculine complex shows significant structural rearrangements from the structures of both the apo and holo forms of the enzyme. It appears that the different rigidity of the protein scaffold contributes to the substrate specificity observed for the two ω-aminotransferases.

PubMed: 23519665
DOI: 10.1107/S0907444912051670

実験手法

X-RAY DIFFRACTION (1.65 Å)