2dor

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[[Image:2dor.gif|left|200px]]<br /><applet load="2dor" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2dor.gif|left|200px]]
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caption="2dor, resolution 2.00&Aring;" />
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'''DIHYDROOROTATE DEHYDROGENASE A FROM LACTOCOCCUS LACTIS COMPLEXED WITH OROTATE'''<br />
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{{Structure
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|PDB= 2dor |SIZE=350|CAPTION= <scene name='initialview01'>2dor</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> and <scene name='pdbligand=ORO:OROTIC ACID'>ORO</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''DIHYDROOROTATE DEHYDROGENASE A FROM LACTOCOCCUS LACTIS COMPLEXED WITH OROTATE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2DOR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis] with <scene name='pdbligand=FMN:'>FMN</scene> and <scene name='pdbligand=ORO:'>ORO</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=2DOR OCA].
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2DOR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DOR OCA].
==Reference==
==Reference==
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The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function., Rowland P, Bjornberg O, Nielsen FS, Jensen KF, Larsen S, Protein Sci. 1998 Jun;7(6):1269-79. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9655329 9655329]
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The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function., Rowland P, Bjornberg O, Nielsen FS, Jensen KF, Larsen S, Protein Sci. 1998 Jun;7(6):1269-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9655329 9655329]
[[Category: Dihydroorotate oxidase]]
[[Category: Dihydroorotate oxidase]]
[[Category: Lactococcus lactis]]
[[Category: Lactococcus lactis]]
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[[Category: pyrimidine nucleotide biosynthesis]]
[[Category: pyrimidine nucleotide biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:29:41 2008''

Revision as of 14:29, 20 March 2008


PDB ID 2dor

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: and
Activity: Dihydroorotate oxidase, with EC number 1.3.3.1
Coordinates: save as pdb, mmCIF, xml



DIHYDROOROTATE DEHYDROGENASE A FROM LACTOCOCCUS LACTIS COMPLEXED WITH OROTATE


Overview

Dihydroorotate dehydrogenases (DHODs) catalyze the oxidation of (S)-dihydroorotate to orotate, the fourth step and only redox reaction in the de novo biosynthesis of pyrimidine nucleotides. A description is given of the crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A (DHODA) complexed with the product of the enzyme reaction orotate. The structure of the complex to 2.0 A resolution has been compared with the structure of the native enzyme. The active site of DHODA is known to contain a water filled cavity buried beneath a highly conserved and flexible loop. In the complex the orotate displaces the water molecules from the active site and stacks above the DHODA flavin isoalloxazine ring, causing only small movements of the surrounding protein residues. The orotate is completely buried beneath the protein surface, and the orotate binding causes a significant reduction in the mobility of the active site loop. The orotate is bound by four conserved asparagine side chains (Asn 67, Asn 127, Asn 132, and Asn 193), the side chains of Lys 43 and Ser 194, and the main chain NH groups of Met 69, Gly 70, and Leu 71. Of these the Lys 43 side chain makes hydrogen bonds to both the flavin isoalloxazine ring and the carboxylate group of the orotate. Potential interactions with bound dihydroorotate are considered using the orotate complex as a basis for molecular modeling. The role of Cys 130 as the active site base is discussed, and the sequence conservation of the active site residues across the different families of DHODs is reviewed, along with implications for differences in substrate binding and in the catalytic mechanisms between these families.

About this Structure

2DOR is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic information is available from OCA.

Reference

The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function., Rowland P, Bjornberg O, Nielsen FS, Jensen KF, Larsen S, Protein Sci. 1998 Jun;7(6):1269-79. PMID:9655329

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