1h82: Difference between revisions
New page: left|200px<br /> <applet load="1h82" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h82, resolution 1.9Å" /> '''STRUCTURE OF POLYAMI... |
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==About this Structure== | ==About this Structure== | ||
1H82 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Zea_mays Zea mays]] with NAG, FAD and GZZ as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.11 1.5.3.11]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H82 OCA]]. | 1H82 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Zea_mays Zea mays]] with NAG, FAD and GZZ as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Polyamine_oxidase Polyamine oxidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.11 1.5.3.11]]. Structure known Active Sites: FAA, FAB, FAC, GZA, GZB and GZC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H82 OCA]]. | ||
==Reference== | ==Reference== | ||
Structural bases for inhibitor binding and catalysis in polyamine oxidase., Binda C, Angelini R, Federico R, Ascenzi P, Mattevi A, Biochemistry. 2001 Mar 6;40(9):2766-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11258887 11258887] | Structural bases for inhibitor binding and catalysis in polyamine oxidase., Binda C, Angelini R, Federico R, Ascenzi P, Mattevi A, Biochemistry. 2001 Mar 6;40(9):2766-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11258887 11258887] | ||
[[Category: Polyamine oxidase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Zea mays]] | [[Category: Zea mays]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
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Revision as of 13:18, 30 October 2007
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STRUCTURE OF POLYAMINE OXIDASE IN COMPLEX WITH GUAZATINE
OverviewOverview
Polyamine oxidase (PAO) carries out the FAD-dependent oxidation of the, secondary amino groups of spermidine and spermine, a key reaction in the, polyamine catabolism. The active site of PAO consists of a 30 A long, U-shaped catalytic tunnel, whose innermost part is located in front of the, flavin ring. To provide insight into the PAO substrate specificity and, amine oxidation mechanism, we have investigated the crystal structure of, maize PAO in the reduced state and in complex with three different, inhibitors, guazatine, 1,8-diaminooctane, and, N(1)-ethyl-N(11)-[(cycloheptyl)methyl]-4,8-diazaundecane (CHENSpm). In the, reduced state, the conformation of the isoalloxazine ring and the, surrounding residues is identical to that of the oxidized enzyme. Only, Lys300 moves away from the ... [(full description)]
About this StructureAbout this Structure
1H82 is a [Single protein] structure of sequence from [Zea mays] with NAG, FAD and GZZ as [ligands]. Active as [Polyamine oxidase], with EC number [1.5.3.11]. Structure known Active Sites: FAA, FAB, FAC, GZA, GZB and GZC. Full crystallographic information is available from [OCA].
ReferenceReference
Structural bases for inhibitor binding and catalysis in polyamine oxidase., Binda C, Angelini R, Federico R, Ascenzi P, Mattevi A, Biochemistry. 2001 Mar 6;40(9):2766-76. PMID:11258887
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