1F8S

CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.

Summary for 1F8S

• Entry DOI: 10.2210/pdb1f8s/pdb
• Related: 1F8R
• Descriptor: L-AMINO ACID OXIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-AMINOBENZOIC ACID, ... (5 entities in total)
• Functional Keywords: flavoenzyme, oxidase, enantiomeric specificity, o-aminobenzoate, active site funnel, helical domain, fad-binding domain, oxidoreductase
• Biological source: Calloselasma rhodostoma (Malayan pit viper)
• Cellular location: Secreted: P81382
• Total number of polymer chains: 8
• Total formula weight: 461739.39

Authors

Pawelek, P.D.,Cheah, J.,Coulombe, R.,Macheroux, P.,Ghisla, S.,Vrielink, A. (deposition date: 2000-07-04, release date: 2000-08-24, Last modification date: 2023-11-15)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)