1f8r: Difference between revisions
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|PDB= 1f8r |SIZE=350|CAPTION= <scene name='initialview01'>1f8r</scene>, resolution 2.00Å | |PDB= 1f8r |SIZE=350|CAPTION= <scene name='initialview01'>1f8r</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
|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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1f8s|1F8S]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f8r OCA], [http://www.ebi.ac.uk/pdbsum/1f8r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f8r RCSB]</span> | |||
}} | }} | ||
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[[Category: Pawelek, P D.]] | [[Category: Pawelek, P D.]] | ||
[[Category: Vrielink, A.]] | [[Category: Vrielink, A.]] | ||
[[Category: active site funnel]] | [[Category: active site funnel]] | ||
[[Category: enantiomeric specificity]] | [[Category: enantiomeric specificity]] | ||
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[[Category: oxidase]] | [[Category: oxidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:18:04 2008'' | ||
Revision as of 20:18, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | , , , | ||||||
| Activity: | L-amino-acid oxidase, with EC number 1.4.3.2 | ||||||
| Related: | 1F8S
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA COMPLEXED WITH CITRATE
OverviewOverview
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 StructureAbout this Structure
1F8R is a Single protein structure of sequence from Calloselasma rhodostoma. Full crystallographic information is available from OCA.
ReferenceReference
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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