2bt1
From Proteopedia
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- | [[Image:2bt1.gif|left|200px]] | + | [[Image:2bt1.gif|left|200px]] |
- | + | ||
- | '''EPSTEIN BARR VIRUS DUTPASE IN COMPLEX WITH A,B-IMINO DUTP''' | + | {{Structure |
+ | |PDB= 2bt1 |SIZE=350|CAPTION= <scene name='initialview01'>2bt1</scene>, resolution 2.70Å | ||
+ | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene> | ||
+ | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=DUP:2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE'>DUP</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/dUTP_diphosphatase dUTP diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.23 3.6.1.23] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''EPSTEIN BARR VIRUS DUTPASE IN COMPLEX WITH A,B-IMINO DUTP''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2BT1 is a [ | + | 2BT1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BT1 OCA]. |
==Reference== | ==Reference== | ||
- | The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases., Tarbouriech N, Buisson M, Seigneurin JM, Cusack S, Burmeister WP, Structure. 2005 Sep;13(9):1299-310. PMID:[http:// | + | The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases., Tarbouriech N, Buisson M, Seigneurin JM, Cusack S, Burmeister WP, Structure. 2005 Sep;13(9):1299-310. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16154087 16154087] |
[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nucleotide metabolism]] | [[Category: nucleotide metabolism]] | ||
[[Category: spine]] | [[Category: spine]] | ||
- | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:06:21 2008'' |
Revision as of 14:06, 20 March 2008
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, resolution 2.70Å | |||||||
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Ligands: | and | ||||||
Activity: | dUTP diphosphatase, with EC number 3.6.1.23 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
EPSTEIN BARR VIRUS DUTPASE IN COMPLEX WITH A,B-IMINO DUTP
Overview
Deoxyuridine 5'-triphosphate pyrophosphatases (dUTPases) are ubiquitous enzymes cleaving dUTP into dUMP and pyrophosphate. They occur as monomeric, dimeric, or trimeric molecules. The trimeric and monomeric enzymes both contain the same five characteristic sequence motifs but in a different order, whereas the dimeric enzymes are not homologous. Monomeric dUTPases only occur in herpesviruses, such as Epstein-Barr virus (EBV). Here, we describe the crystal structures of EBV dUTPase in complex with the product dUMP and a substrate analog alpha,beta-imino-dUTP. The molecule consists of three domains forming one active site that has a structure extremely similar to one of the three active sites of trimeric dUTPases. The three domains functionally correspond to the subunits of the trimeric form. Domains I and II have the dUTPase fold, but they differ considerably in the regions that are not involved in the formation of the unique active site, whereas domain III has only little secondary structure.
About this Structure
2BT1 is a Single protein structure of sequence from Human herpesvirus 4. Full crystallographic information is available from OCA.
Reference
The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases., Tarbouriech N, Buisson M, Seigneurin JM, Cusack S, Burmeister WP, Structure. 2005 Sep;13(9):1299-310. PMID:16154087
Page seeded by OCA on Thu Mar 20 16:06:21 2008
Categories: Human herpesvirus 4 | Single protein | DUTP diphosphatase | Buisson, M. | Burmeister, W P. | Cusack, S. | SPINE, Structural Proteomics in Europe. | Seigneurin, J M. | Tarbouriech, N. | DUP | MG | Dutpase | Hydrolase | Monomer | Nucleotide metabolism | Spine | Structural genomic | Structural proteomics in europe