2YR6

Crystal structure of L-phenylalanine oxidase from Psuedomonas sp.P501

2YR6 の概要

• エントリーDOI: 10.2210/pdb2yr6/pdb
• 関連するPDBエントリー: 2YR4 2YR5 2YR7 2YR8 2YR9
• 分子名称: Pro-enzyme of L-phenylalanine oxidase, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total)
• 機能のキーワード: l-phenylalanine oxidase, amino oxidase, flavoenzyme, oxidoreductase
• 由来する生物種: Pseudomonas sp. P-501
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 158021.01

構造登録者

Ida, K.,Kurabayashi, M.,Suguro, M.,Suzuki, H. (登録日: 2007-04-02, 公開日: 2008-04-15, 最終更新日: 2023-11-15)

主引用文献

Ida, K.,Kurabayashi, M.,Suguro, M.,Hiruma, Y.,Hikima, T.,Yamomoto, M.,Suzuki, H.
Structural basis of proteolytic activation of L-phenylalanine oxidase from Pseudomonas sp. P-501.
J.Biol.Chem., 283:16584-16590, 2008

PubMed Abstract: The mature form of l-phenylalanine oxidase (PAOpt) from Pseudomonas sp. P-501 was generated and activated by the proteolytic cleavage of a noncatalytic proenzyme (proPAO). The crystal structures of proPAO, PAOpt, and the PAOpt-o-amino benzoate (AB) complex were determined at 1.7, 1.25, and 1.35A resolutions, respectively. The structure of proPAO suggests that the prosequence peptide of proPAO occupies the funnel (pathway) of the substrate amino acid from the outside of the protein to the interior flavin ring, whereas the funnel is closed with the hydrophobic residues at its vestibule in both PAOpt and the PAOpt-AB complex. All three structures have an oxygen channel that is open to the surface of the protein from the flavin ring. These results suggest that structural changes were induced by proteolysis; that is, the proteolysis of proPAO removes the prosequence and closes the funnel to keep the active site hydrophobic but keeps the oxygen channel open. The possibility that an interaction of the hydrophobic side chain of substrate with the residues of the vestibule region may open the funnel as a putative amino acid channel is discussed.

PubMed: 18417467
DOI: 10.1074/jbc.M800366200

実験手法

X-RAY DIFFRACTION (1.35 Å)