1gte: Difference between revisions
New page: left|200px<br /> <applet load="1gte" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gte, resolution 1.65Å" /> '''DIHYDROPYRIMIDINE D... |
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==About this Structure== | ==About this Structure== | ||
1GTE 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 SF4, FMN, FAD and IUR 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=1.3.1.2 1.3.1.2]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GTE OCA]]. | 1GTE 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 SF4, FMN, FAD and IUR as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Dihydropyrimidine_dehydrogenase_(NADP(+)) Dihydropyrimidine dehydrogenase (NADP(+))]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.2 1.3.1.2]]. Structure known Active Site: FA1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GTE OCA]]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer., Dobritzsch D, Ricagno S, Schneider G, Schnackerz KD, Lindqvist Y, J Biol Chem. 2002 Apr 12;277(15):13155-66. Epub 2002 Jan 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11796730 11796730] | Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer., Dobritzsch D, Ricagno S, Schneider G, Schnackerz KD, Lindqvist Y, J Biol Chem. 2002 Apr 12;277(15):13155-66. Epub 2002 Jan 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11796730 11796730] | ||
[[Category: Dihydropyrimidine dehydrogenase (NADP(+))]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: pyrimidine catabolism]] | [[Category: pyrimidine catabolism]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:17:52 2007'' | ||
Revision as of 14:13, 30 October 2007
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DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG, BINARY COMPLEX WITH 5-IODOURACIL
OverviewOverview
Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step, in pyrimidine degradation by converting pyrimidines to the corresponding, 5,6- dihydro compounds. The three-dimensional structures of a binary, complex with the inhibitor 5-iodouracil and two ternary complexes with, NADPH and the inhibitors 5-iodouracil and uracil-4-acetic acid were, determined by x-ray crystallography. In the ternary complexes, NADPH is, bound in a catalytically competent fashion, with the nicotinamide ring in, a position suitable for hydride transfer to FAD. The structures provide a, complete picture of the electron transfer chain from NADPH to the, substrate, 5-iodouracil, spanning a distance of 56 A and involving FAD, four [Fe-S] clusters, and FMN as cofactors. The crystallographic analysis, ... [(full description)]
About this StructureAbout this Structure
1GTE is a [Single protein] structure of sequence from [Sus scrofa] with SF4, FMN, FAD and IUR as [ligands]. Active as [Dihydropyrimidine dehydrogenase (NADP(+))], with EC number [1.3.1.2]. Structure known Active Site: FA1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer., Dobritzsch D, Ricagno S, Schneider G, Schnackerz KD, Lindqvist Y, J Biol Chem. 2002 Apr 12;277(15):13155-66. Epub 2002 Jan 16. PMID:11796730
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