Deoxyuridine 5'-triphosphate nucleotidohydrolase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 13: Line 13:
The <scene name='48/488500/Cv/5'>active site</scene> contains Mg<sup>+2</sup> ions which are essensial for DUTP activity. The <scene name='48/488500/Cv/6'>Mg+2 ions are hexacoordinated to acidic residues and water molecules</scene>.<ref>PMID:15364583</ref> Water molecules are labeled Wa.
The <scene name='48/488500/Cv/5'>active site</scene> contains Mg<sup>+2</sup> ions which are essensial for DUTP activity. The <scene name='48/488500/Cv/6'>Mg+2 ions are hexacoordinated to acidic residues and water molecules</scene>.<ref>PMID:15364583</ref> Water molecules are labeled Wa.
 +
 +
==3D structures of dUTPase==
 +
[[dUTPase 3D structures]]
 +
</StructureSection>
</StructureSection>
==3D structures of dUTPase==
==3D structures of dUTPase==
Line 21: Line 25:
*DUTP
*DUTP
 +
**[[1q5u]] - hDUTP – human<br />
**[[1dup]], [[1eu5]], [[1euw]] – EcDUTP – ''Escherichia coli''<br />
**[[1dup]], [[1eu5]], [[1euw]] – EcDUTP – ''Escherichia coli''<br />
**[[1dun]] – EvDUTP – Equine infectious anemia virus<br />
**[[1dun]] – EvDUTP – Equine infectious anemia virus<br />
Line 34: Line 39:
**[[2xx6]] - BsDUTP – ''Bacillus subtilis''<br />
**[[2xx6]] - BsDUTP – ''Bacillus subtilis''<br />
**[[3tqz]] - DUTP – ''Coxiella burnetii''<br />
**[[3tqz]] - DUTP – ''Coxiella burnetii''<br />
-
**[[1q5u]] - hDUTP – human<br />
 
**[[4lhr]] - DUTP – ''Burkholderia thailandensis''<br />
**[[4lhr]] - DUTP – ''Burkholderia thailandensis''<br />
**[[3h6x]] - DUTP – ''Streptococcus mutans''<br />
**[[3h6x]] - DUTP – ''Streptococcus mutans''<br />
**[[5myf]] - SaDUTP – ''Staphylococcus aureus''<br />
**[[5myf]] - SaDUTP – ''Staphylococcus aureus''<br />
**[[5myi]] - SaDUTP (mutant)<br />
**[[5myi]] - SaDUTP (mutant)<br />
 +
**[[6mai]] - LpDUTP – ''Legionella pneumophila''<br />
*DUTP binary complexes
*DUTP binary complexes
 +
**[[4mz5]], [[4mz6]] – hDUTP + importin subunit α-1<br />
 +
**[[5h4j]] - hDUTP + inhibitor<br />
**[[1dud]] – EcDUTP + dUDP<br />
**[[1dud]] – EcDUTP + dUDP<br />
**[[2hrm]] - EcDUTP + dUTP derivative<br />
**[[2hrm]] - EcDUTP + dUTP derivative<br />
Line 61: Line 68:
**[[3tq5]], [[3trl]], [[3trn]], [[3ts6]], [[3tsl]], [[3tta]] - MPmvDUTP catalytic domain (mutant) + dUMP<br />
**[[3tq5]], [[3trl]], [[3trn]], [[3ts6]], [[3tsl]], [[3tta]] - MPmvDUTP catalytic domain (mutant) + dUMP<br />
**[[4ooq]], [[2pc5]] – AtDUTP + Mg – ''Arabidopsis thaliana''<br />
**[[4ooq]], [[2pc5]] – AtDUTP + Mg – ''Arabidopsis thaliana''<br />
-
**[[4mz5]], [[4mz6]] – hDUTP + importin subunit α-1<br />
 
-
**[[5h4j]] - hDUTP + inhibitor<br />
 
**[[3zf0]], [[3zf1]], [[3zf2]], [[3zf3]], [[3zf4]], [[3zf5]], [[3zf6]], [[5cct]], [[5nyz]], [[5nz2]] - SpDUTP (mutant) + dUTP derivative – ''Staphylococcus'' phage 80α<br />
**[[3zf0]], [[3zf1]], [[3zf2]], [[3zf3]], [[3zf4]], [[3zf5]], [[3zf6]], [[5cct]], [[5nyz]], [[5nz2]] - SpDUTP (mutant) + dUTP derivative – ''Staphylococcus'' phage 80α<br />
**[[5cco]] - SpDUTP + dUMP <br />
**[[5cco]] - SpDUTP + dUMP <br />
Line 68: Line 73:
**[[4wrk]] - DUTP (mutant) + dUTP derivative – ''Staphylococcus'' phage φ11<br />
**[[4wrk]] - DUTP (mutant) + dUTP derivative – ''Staphylococcus'' phage φ11<br />
**[[5myd]] - DUTP + dUTP derivative – ''Staphylococcus'' <br />
**[[5myd]] - DUTP + dUTP derivative – ''Staphylococcus'' <br />
 +
**[[6mao]] - LpDUTP + dUMP <br />
*DUTP ternary complexes
*DUTP ternary complexes

Revision as of 08:56, 5 June 2019

dUTPase complex with dUTP analog and Mg+2 ions (green) (PDB entry 1w2y)

Drag the structure with the mouse to rotate

3D structures of dUTPase

Updated on 05-June-2019

References

  1. Vertessy BG, Toth J. Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases. Acc Chem Res. 2009 Jan 20;42(1):97-106. PMID:18837522 doi:10.1021/ar800114w
  2. Moroz OV, Harkiolaki M, Galperin MY, Vagin AA, Gonzalez-Pacanowska D, Wilson KS. The crystal structure of a complex of Campylobacter jejuni dUTPase with substrate analogue sheds light on the mechanism and suggests the "basic module" for dimeric d(C/U)TPases. J Mol Biol. 2004 Oct 1;342(5):1583-97. PMID:15364583 doi:10.1016/j.jmb.2004.07.050

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Personal tools