1F8R

CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA COMPLEXED WITH CITRATE

1F8R の概要

• エントリーDOI: 10.2210/pdb1f8r/pdb
• 関連するPDBエントリー: 1F8S
• 分子名称: L-AMINO ACID OXIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: flavoenzyme, oxidase, enantiomeric specificity, active site funnel, helical domain, fad-binding domain, oxidoreductase
• 由来する生物種: Calloselasma rhodostoma (Malayan pit viper)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 232274.73

構造登録者

Pawelek, P.D.,Cheah, J.,Coulombe, R.,Macheroux, P.,Ghisla, S.,Vrielink, A. (登録日: 2000-07-04, 公開日: 2000-08-24, 最終更新日: 2024-11-13)

主引用文献

Pawelek, P.D.,Cheah, J.,Coulombe, R.,Macheroux, P.,Ghisla, S.,Vrielink, A.
The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site.
EMBO J., 19:4204-4215, 2000

PubMed Abstract: The structure of L-amino acid oxidase (LAAO) from Calloselasma rhodostoma has been determined to 2.0 A resolution in the presence of two ligands: citrate and o-aminobenzoate (AB). The protomer consists of three domains: an FAD-binding domain, a substrate-binding domain and a helical domain. The interface between the substrate-binding and helical domains forms a 25 A long funnel, which provides access to the active site. Three AB molecules are visible within the funnel of the LAAO-AB complex; their orientations suggest the trajectory of the substrate to the active site. The innermost AB molecule makes hydrogen bond contacts with the active site residues, Arg90 and Gly464, and the aromatic portion of the ligand is situated in a hydrophobic pocket. These contacts are proposed to mimic those of the natural substrate. Comparison of LAAO with the structure of mammalian D-amino acid oxidase reveals significant differences in their modes of substrate entry. Furthermore, a mirror-symmetrical relationship between the two substrate-binding sites is observed which facilitates enantiomeric selectivity while preserving a common arrangement of the atoms involved in catalysis.

PubMed: 10944103
DOI: 10.1093/emboj/19.16.4204

実験手法

X-RAY DIFFRACTION (2 Å)