1f8s
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1f8s.jpg|left|200px]] | [[Image:1f8s.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1f8s", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1f8s| PDB=1f8s | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.''' | '''CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.''' | ||
| Line 32: | Line 29: | ||
[[Category: Pawelek, P D.]] | [[Category: Pawelek, P D.]] | ||
[[Category: Vrielink, A.]] | [[Category: Vrielink, A.]] | ||
| - | [[Category: | + | [[Category: Active site funnel]] |
| - | [[Category: | + | [[Category: Enantiomeric specificity]] |
| - | [[Category: | + | [[Category: Fad-binding domain]] |
| - | [[Category: | + | [[Category: Flavoenzyme]] |
| - | [[Category: | + | [[Category: Helical domain]] |
| - | [[Category: | + | [[Category: O-aminobenzoate]] |
| - | [[Category: | + | [[Category: Oxidase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:02:12 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:02, 2 May 2008
CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.
Overview
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.
About this Structure
1F8S is a Single protein structure of sequence from Calloselasma rhodostoma. Full crystallographic information is available from OCA.
Reference
The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site., Pawelek PD, Cheah J, Coulombe R, Macheroux P, Ghisla S, Vrielink A, EMBO J. 2000 Aug 15;19(16):4204-15. PMID:10944103 Page seeded by OCA on Fri May 2 16:02:12 2008
