1M32

Crystal Structure of 2-aminoethylphosphonate Transaminase

1M32 の概要

• エントリーDOI: 10.2210/pdb1m32/pdb
• 分子名称: 2-aminoethylphosphonate-pyruvate aminotransferase, PYRIDOXAL-5'-PHOSPHATE, PHOSPHONOACETALDEHYDE, ... (5 entities in total)
• 機能のキーワード: plp-dependent aminotransferase fold, transferase
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 246163.33

構造登録者

Chen, C.C.H.,Zhang, H.,Kim, A.D.,Howard, A.,Sheldrick, G.M.,Mariano-Dunnaway, D.,Herzberg, O. (登録日: 2002-06-26, 公開日: 2002-11-20, 最終更新日: 2025-03-26)

主引用文献

Chen, C.C.H.,Zhang, H.,Kim, A.D.,Howard, A.,Sheldrick, G.M.,Mariano-Dunnaway, D.,Herzberg, O.
Degradation Pathway of the Phosphonate Ciliatine: Crystal Structure of 2-Aminoethylphosphonate Transaminase
Biochemistry, 41:13162-13169, 2002

PubMed Abstract: Phosphonates allow certain organisms to thrive in otherwise hostile environments, and 2-aminoethylphosphonate (AEP) is a precursor of many cellular phosphonates. AEP transaminase (AEPT) is an enzyme essential to phosphonate synthesis and degradation pathways. The crystal structure of AEP transaminase was determined by multiwavelength anomalous diffraction of 66 selenium atoms. The refined structure at 2.2 A resolution revealed an overall fold and active site location similar to those of the dimeric, two-domain structure of type I aminotransferases. The active site contains a cofactor, pyridoxal 5'-phosphate (PLP), and the product phosphonoacetaldehyde. Comparison with other type I aminotransferase structures shows that the PLP-protein interactions are conserved. Modeling of bound substrates and products reveals the structural basis for AEP recognition and the stereospecificity of proton elimination at the alpha-carbon and indicates conformational changes along the reaction pathway.

PubMed: 12403617
DOI: 10.1021/bi026231v

実験手法

X-RAY DIFFRACTION (2.2 Å)