1f76
From Proteopedia
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[[Image:1f76.jpg|left|200px]] | [[Image:1f76.jpg|left|200px]] | ||
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| - | | | + | {{STRUCTURE_1f76| PDB=1f76 | SCENE= }} |
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'''ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE''' | '''ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F76 is a [[Single protein]] structure | + | 1F76 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F76 OCA]. |
==Reference== | ==Reference== | ||
E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases., Norager S, Jensen KF, Bjornberg O, Larsen S, Structure. 2002 Sep;10(9):1211-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12220493 12220493] | E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases., Norager S, Jensen KF, Bjornberg O, Larsen S, Structure. 2002 Sep;10(9):1211-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12220493 12220493] | ||
| - | [[Category: ]] | ||
[[Category: Dihydroorotate oxidase]] | [[Category: Dihydroorotate oxidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Larsen, S.]] | [[Category: Larsen, S.]] | ||
[[Category: Norager, S.]] | [[Category: Norager, S.]] | ||
| - | [[Category: | + | [[Category: Alpha-beta-barrel]] |
| - | [[Category: | + | [[Category: Fmn binding domain]] |
| - | [[Category: | + | [[Category: Monomer]] |
| - | [[Category: | + | [[Category: Orotate complex]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:59:07 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:59, 2 May 2008
ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE
Overview
The flavoenzymes dihydroorotate dehydrogenases (DHODs) catalyze the fourth and only redox step in the de novo biosynthesis of UMP. Enzymes belonging to class 2, according to their amino acid sequence, are characterized by having a serine residue as the catalytic base and a longer N terminus. The structure of class 2 E. coli DHOD, determined by MAD phasing, showed that the N-terminal extension forms a separate domain. The catalytic serine residue has an environment differing from the equivalent cysteine in class 1 DHODs. Significant differences between the two classes of DHODs were identified by comparison of the E. coli DHOD with the other known DHOD structures, and differences with the class 2 human DHOD explain the variation in their inhibitors.
About this Structure
1F76 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases., Norager S, Jensen KF, Bjornberg O, Larsen S, Structure. 2002 Sep;10(9):1211-23. PMID:12220493 Page seeded by OCA on Fri May 2 15:59:07 2008
