1h7w
From Proteopedia
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| - | [[Image:1h7w. | + | [[Image:1h7w.jpg|left|200px]]<br /><applet load="1h7w" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1h7w" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1h7w, resolution 1.90Å" /> | caption="1h7w, resolution 1.90Å" /> | ||
'''DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG'''<br /> | '''DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H7W 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 and FAD 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] | + | 1H7W 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 and FAD 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] Known structural/functional Sites: <scene name='pdbsite=AC5:Fmn Binding Site For Chain A'>AC5</scene>, <scene name='pdbsite=AC6:Fad Binding Site For Chain A'>AC6</scene>, <scene name='pdbsite=BC5:Fmn Binding Site For Chain B'>BC5</scene>, <scene name='pdbsite=BC6:Fad Binding Site For Chain B'>BC6</scene>, <scene name='pdbsite=CC5:Fmn Binding Site For Chain C'>CC5</scene>, <scene name='pdbsite=CC6:Fad Binding Site For Chain C'>CC6</scene>, <scene name='pdbsite=DC5:Fmn Binding Site For Chain D'>DC5</scene> and <scene name='pdbsite=DC6:Fad Binding Site For Chain D'>DC6</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H7W OCA]. |
==Reference== | ==Reference== | ||
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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 Dec 18 16:07:40 2007'' |
Revision as of 13:57, 18 December 2007
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DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG
Overview
Dihydropyrimidine dehydrogenase catalyzes the first step in pyrimidine, degradation: the NADPH-dependent reduction of uracil and thymine to the, corresponding 5,6-dihydropyrimidines. Its controlled inhibition has become, an adjunct target for cancer therapy, since the enzyme is also responsible, for the rapid breakdown of the chemotherapeutic drug 5-fluorouracil. The, crystal structure of the homodimeric pig liver enzyme (2x 111 kDa), determined at 1.9 A resolution reveals a highly modular subunit, organization, consisting of five domains with different folds., Dihydropyrimidine dehydrogenase contains two FAD, two FMN and eight, [4Fe-4S] clusters, arranged in two electron transfer chains that pass the, dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved, coordination involving a glutamine residue. The ternary complex of an, inactive mutant of the enzyme with bound NADPH and 5-fluorouracil reveals, the architecture of the substrate-binding sites and residues responsible, for recognition and binding of the drug.
About this Structure
1H7W is a Single protein structure of sequence from Sus scrofa with SF4, FMN and FAD as ligands. Active as Dihydropyrimidine dehydrogenase (NADP(+)), with EC number 1.3.1.2 Known structural/functional Sites: , , , , , , and . Full crystallographic information is available from OCA.
Reference
Crystal structure of dihydropyrimidine dehydrogenase, a major determinant of the pharmacokinetics of the anti-cancer drug 5-fluorouracil., Dobritzsch D, Schneider G, Schnackerz KD, Lindqvist Y, EMBO J. 2001 Feb 15;20(4):650-60. PMID:11179210
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