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1f76

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[[Image:1f76.jpg|left|200px]]
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{{Seed}}
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[[Image:1f76.png|left|200px]]
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{{STRUCTURE_1f76| PDB=1f76 | SCENE= }}
{{STRUCTURE_1f76| PDB=1f76 | SCENE= }}
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'''ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE'''
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===ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12220493 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12220493}}
==About this Structure==
==About this Structure==
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[[Category: Monomer]]
[[Category: Monomer]]
[[Category: Orotate complex]]
[[Category: Orotate complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:48:36 2008''

Revision as of 23:48, 30 June 2008

Image:1f76.png

Template:STRUCTURE 1f76

ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE

Template:ABSTRACT PUBMED 12220493

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 Tue Jul 1 02:48:36 2008

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