1f8r: Difference between revisions
New page: left|200px<br /><applet load="1f8r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f8r, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1f8r.gif|left|200px]]<br /><applet load="1f8r" size=" | [[Image:1f8r.gif|left|200px]]<br /><applet load="1f8r" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1f8r, resolution 2.00Å" /> | caption="1f8r, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA COMPLEXED WITH CITRATE'''<br /> | '''CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA COMPLEXED WITH CITRATE'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of L-amino acid oxidase (LAAO) from Calloselasma rhodostoma | 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== | ==About this Structure== | ||
1F8R 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 NAG, CIT and FAD 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:// | 1F8R 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=CIT:'>CIT</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=1F8R OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Ghisla, S.]] | [[Category: Ghisla, S.]] | ||
[[Category: Macheroux, P.]] | [[Category: Macheroux, P.]] | ||
[[Category: Pawelek, P | [[Category: Pawelek, P D.]] | ||
[[Category: Vrielink, A.]] | [[Category: Vrielink, A.]] | ||
[[Category: CIT]] | [[Category: CIT]] | ||
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[[Category: oxidase]] | [[Category: oxidase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:03 2008'' | ||
Revision as of 13:36, 21 February 2008
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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 with , and as ligands. Active as L-amino-acid oxidase, with EC number 1.4.3.2 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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