1an9

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(New page: 200px<br /><applet load="1an9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1an9, resolution 2.5&Aring;" /> '''D-AMINO ACID OXIDASE ...)
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'''D-AMINO ACID OXIDASE COMPLEX WITH O-AMINOBENZOATE'''<br />
'''D-AMINO ACID OXIDASE COMPLEX WITH O-AMINOBENZOATE'''<br />
==Overview==
==Overview==
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As an extension of our recent X-ray crystallographic determination of the, tertiary structure of D-amino acid oxidase (DAO) [Mizutani, H. et al., (1996) J. Biochem. 120, 14-17], we solved the crystal structure of the, complex of DAO with a substrate analog, o-aminobenzoate (OAB). The, alignment between flavin and OAB in the crystal structure of the complex, is consistent with charge-transfer interaction through the overlap between, the highest occupied molecular orbital of OAB and the lowest unoccupied, molecular orbital of flavin. Starting with the atomic coordinates of this, complex as the initial model, we carried out molecular mechanics, simulation for the DAO-D-leucine complex and thus obtained a model for the, enzyme-substrate complex. According to the enzyme-substrate complex model, the alpha-proton is pointed toward N(5) of flavin while the lone-pair of, the substrate amino group can approach C(4a) of flavin within an, interacting distance. This model as well as DAO-OAB complex enables the, evaluation of the substrate-flavin interaction prior to electron transfer, from the substrate to flavin and provides two possible mechanisms for the, reductive-half reaction of DAO, i.e., the electron-proton-electron, transfer mechanism and the ionic mechanism.
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As an extension of our recent X-ray crystallographic determination of the tertiary structure of D-amino acid oxidase (DAO) [Mizutani, H. et al. (1996) J. Biochem. 120, 14-17], we solved the crystal structure of the complex of DAO with a substrate analog, o-aminobenzoate (OAB). The alignment between flavin and OAB in the crystal structure of the complex is consistent with charge-transfer interaction through the overlap between the highest occupied molecular orbital of OAB and the lowest unoccupied molecular orbital of flavin. Starting with the atomic coordinates of this complex as the initial model, we carried out molecular mechanics simulation for the DAO-D-leucine complex and thus obtained a model for the enzyme-substrate complex. According to the enzyme-substrate complex model, the alpha-proton is pointed toward N(5) of flavin while the lone-pair of the substrate amino group can approach C(4a) of flavin within an interacting distance. This model as well as DAO-OAB complex enables the evaluation of the substrate-flavin interaction prior to electron transfer from the substrate to flavin and provides two possible mechanisms for the reductive-half reaction of DAO, i.e., the electron-proton-electron transfer mechanism and the ionic mechanism.
==About this Structure==
==About this Structure==
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1AN9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with FAD and BE2 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AN9 OCA].
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1AN9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=BE2:'>BE2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/D-amino-acid_oxidase D-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.3 1.4.3.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN9 OCA].
==Reference==
==Reference==
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Structural and mechanistic studies on D-amino acid oxidase x substrate complex: implications of the crystal structure of enzyme x substrate analog complex., Miura R, Setoyama C, Nishina Y, Shiga K, Mizutani H, Miyahara I, Hirotsu K, J Biochem (Tokyo). 1997 Oct;122(4):825-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9399588 9399588]
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Structural and mechanistic studies on D-amino acid oxidase x substrate complex: implications of the crystal structure of enzyme x substrate analog complex., Miura R, Setoyama C, Nishina Y, Shiga K, Mizutani H, Miyahara I, Hirotsu K, J Biochem. 1997 Oct;122(4):825-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9399588 9399588]
[[Category: D-amino-acid oxidase]]
[[Category: D-amino-acid oxidase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:58:37 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:18 2008''

Revision as of 09:46, 21 February 2008

Image:1an9.gif

1an9, resolution 2.5Å

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D-AMINO ACID OXIDASE COMPLEX WITH O-AMINOBENZOATE

Overview

As an extension of our recent X-ray crystallographic determination of the tertiary structure of D-amino acid oxidase (DAO) [Mizutani, H. et al. (1996) J. Biochem. 120, 14-17], we solved the crystal structure of the complex of DAO with a substrate analog, o-aminobenzoate (OAB). The alignment between flavin and OAB in the crystal structure of the complex is consistent with charge-transfer interaction through the overlap between the highest occupied molecular orbital of OAB and the lowest unoccupied molecular orbital of flavin. Starting with the atomic coordinates of this complex as the initial model, we carried out molecular mechanics simulation for the DAO-D-leucine complex and thus obtained a model for the enzyme-substrate complex. According to the enzyme-substrate complex model, the alpha-proton is pointed toward N(5) of flavin while the lone-pair of the substrate amino group can approach C(4a) of flavin within an interacting distance. This model as well as DAO-OAB complex enables the evaluation of the substrate-flavin interaction prior to electron transfer from the substrate to flavin and provides two possible mechanisms for the reductive-half reaction of DAO, i.e., the electron-proton-electron transfer mechanism and the ionic mechanism.

About this Structure

1AN9 is a Single protein structure of sequence from Sus scrofa with and as ligands. Active as D-amino-acid oxidase, with EC number 1.4.3.3 Full crystallographic information is available from OCA.

Reference

Structural and mechanistic studies on D-amino acid oxidase x substrate complex: implications of the crystal structure of enzyme x substrate analog complex., Miura R, Setoyama C, Nishina Y, Shiga K, Mizutani H, Miyahara I, Hirotsu K, J Biochem. 1997 Oct;122(4):825-33. PMID:9399588

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