1f76
From Proteopedia
(New page: 200px<br /><applet load="1f76" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f76, resolution 2.5Å" /> '''ESCHERICHIA COLI DIHY...) |
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| - | [[Image:1f76.jpg|left|200px]]<br /><applet load="1f76" size=" | + | [[Image:1f76.jpg|left|200px]]<br /><applet load="1f76" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f76, resolution 2.5Å" /> | caption="1f76, resolution 2.5Å" /> | ||
'''ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE'''<br /> | '''ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The flavoenzymes dihydroorotate dehydrogenases (DHODs) catalyze the fourth | + | 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== | ==About this Structure== | ||
| - | 1F76 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with FMN, ORO and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydroorotate_oxidase Dihydroorotate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.1 1.3.3.1] Full crystallographic information is available from [http:// | + | 1F76 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=FMN:'>FMN</scene>, <scene name='pdbligand=ORO:'>ORO</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydroorotate_oxidase Dihydroorotate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.1 1.3.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F76 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bjornberg, O.]] | [[Category: Bjornberg, O.]] | ||
| - | [[Category: Jensen, K | + | [[Category: Jensen, K F.]] |
[[Category: Larsen, S.]] | [[Category: Larsen, S.]] | ||
[[Category: Norager, S.]] | [[Category: Norager, S.]] | ||
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[[Category: orotate complex]] | [[Category: orotate complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:43 2008'' |
Revision as of 10:35, 21 February 2008
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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 of sequence from [1] with , and as ligands. Active as Dihydroorotate oxidase, with EC number 1.3.3.1 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 [[Category: ]]
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