1f8s

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[[Image:1f8s.jpg|left|200px]]<br /><applet load="1f8s" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1f8s.jpg|left|200px]]
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caption="1f8s, resolution 2.00&Aring;" />
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'''CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.'''<br />
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{{Structure
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|PDB= 1f8s |SIZE=350|CAPTION= <scene name='initialview01'>1f8s</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=BE2:2-AMINOBENZOIC+ACID'>BE2</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1F8S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Calloselasma_rhodostoma Calloselasma rhodostoma] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=BE2:'>BE2</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F8S OCA].
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1F8S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Calloselasma_rhodostoma Calloselasma rhodostoma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F8S OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10944103 10944103]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10944103 10944103]
[[Category: Calloselasma rhodostoma]]
[[Category: Calloselasma rhodostoma]]
[[Category: L-amino-acid oxidase]]
[[Category: L-amino-acid oxidase]]
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[[Category: oxidase]]
[[Category: oxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:05:54 2008''

Revision as of 09:05, 20 March 2008

Image:1f8s.jpg


PDB ID 1f8s

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , and
Activity: L-amino-acid oxidase, with EC number 1.4.3.2
Coordinates: save as pdb, mmCIF, xml



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

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