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1f76

From Proteopedia

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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===
===ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE===
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{{ABSTRACT_PUBMED_12220493}}
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==Function==
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[[http://www.uniprot.org/uniprot/PYRD_ECOLI PYRD_ECOLI]] Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.<ref>PMID:10074342</ref>
==About this Structure==
==About this Structure==
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[[1f76]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F76 OCA].
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[[1f76]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/9bact 9bact]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F76 OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:012220493</ref><references group="xtra"/>
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<ref group="xtra">PMID:012220493</ref><references group="xtra"/><references/>
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[[Category: Bacteria]]
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[[Category: 9bact]]
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[[Category: Dihydroorotate oxidase]]
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[[Category: Bjornberg, O.]]
[[Category: Bjornberg, O.]]
[[Category: Jensen, K F.]]
[[Category: Jensen, K F.]]

Revision as of 13:43, 12 March 2014

Template:STRUCTURE 1f76

Contents

ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE

Template:ABSTRACT PUBMED 12220493

Function

[PYRD_ECOLI] Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.[1]

About this Structure

1f76 is a 4 chain structure with sequence from 9bact. Full crystallographic information is available from OCA.

Reference

  • Norager S, Jensen KF, Bjornberg O, Larsen S. E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases. Structure. 2002 Sep;10(9):1211-23. PMID:12220493
  1. ↑ Bjornberg O, Gruner AC, Roepstorff P, Jensen KF. The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis. Biochemistry. 1999 Mar 9;38(10):2899-908. PMID:10074342 doi:http://dx.doi.org/10.1021/bi982352c

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