2EFU

The crystal structure of D-amino acid amidase from Ochrobactrum anthropi SV3 complexed with L-phenylalanine

2EFU の概要

• エントリーDOI: 10.2210/pdb2efu/pdb
• 関連するPDBエントリー: 2efx
• 分子名称: D-Amino acid amidase, BARIUM ION, PHENYLALANINE, ... (4 entities in total)
• 機能のキーワード: penicillin recognizing proteins, d-stereospecific, amidase, l-phenylalanine, hydrolase
• 由来する生物種: Ochrobactrum anthropi
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 245187.45

構造登録者

Okazaki, S.,Suzuki, A.,Mizushima, T.,Komeda, H.,Asano, Y.,Yamane, T. (登録日: 2007-02-26, 公開日: 2007-03-06, 最終更新日: 2023-10-25)

主引用文献

Okazaki, S.,Suzuki, A.,Mizushima, T.,Komeda, H.,Asano, Y.,Yamane, T.
Structures of D-amino-acid amidase complexed with L-phenylalanine and with L-phenylalanine amide: insight into the D-stereospecificity of D-amino-acid amidase from Ochrobactrum anthropi SV3.
Acta Crystallogr.,Sect.D, 64:331-334, 2008

PubMed Abstract: The crystal structures of D-amino-acid amidase (DAA) from Ochrobactrum anthropi SV3 in complex with L-phenylalanine and with L-phenylalanine amide were determined at 2.3 and 2.2 A resolution, respectively. Comparison of the L-phenylalanine amide complex with the D-phenylalanine complex reveals that the D-stereospecificity of DAA might be achieved as a consequence of three structural factors: (i) the hydrophobic cavity in the region in which the hydrophobic side chain of the substrate is held, (ii) the spatial arrangement of Gln310 O and Glu114 O epsilon2 that fixes the amino N atom of the substrate and (iii) the existence of two cavities that keep the carboxyl/amide group of the substrate near or apart from Ser60 O gamma.

PubMed: 18323628
DOI: 10.1107/S0907444907067479

実験手法

X-RAY DIFFRACTION (2.3 Å)