FunctionDeoxyuridine 5’-triphosphate nucleotidohydrolase (DUTP) catalyzes the conversion of dUTP to dUMP and pyrophosphate (PPi). DUTP plays a key role in keeping significant amounts of dUTP from the DNA synthesis pathway.
Prokaryotic DUTP contains metal ion. [1]
RelevanceDUTP inhibitors are being tested as possible anti-bacterial agents targeting diseases like malaria, leishmaniasis, tuberculosis and trypanosomiasis.
Structural highlightsThe contains Mg+2 ions which are essensial for DUTP activity. The .[2] Water molecules are labeled Wa.
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3D structures of dUTPase3D structures of dUTPase
Updated on 21-February-2019
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- DUTP
- 1dup, 1eu5, 1euw – EcDUTP – Escherichia coli
- 1dun – EvDUTP – Equine infectious anemia virus
- 1mq7 – MtDUTP – Mycobacterium tuberculosis
- 4gk6 - DUTP – Mycobacterium abscessus
- 1ogl – TcDUTP – Trypanosoma cruzi
- 2d4l - MPmvDUTP residues 83-234 – Mason_Pfizer monkey virus
- 2d4m - MPmvDUTP residues 83-234 (mutant)
- 2okb, 2okd - VvDUTP – Vaccinia virus
- 3hhq - yDUTP – yeast
- 3lqw - DUTP – Entamoeba histolytica
- 3mbq, 3mdx - DUTP – Brucella melitensis
- 2xx6 - BsDUTP – Bacillus subtilis
- 3tqz - DUTP – Coxiella burnetii
- 1q5u - hDUTP – human
- 4lhr - DUTP – Burkholderia thailandensis
- 3h6x - DUTP – Streptococcus mutans
- 5myf - SaDUTP – Staphylococcus aureus
- 5myi - SaDUTP (mutant)
- DUTP binary complexes
- 1dud – EcDUTP + dUDP
- 2hrm - EcDUTP + dUTP derivative
- 1seh - EcDUTP + dUMP
- 3f4f - yDUTP + dUMP
- 1dut – DUTP + Mg – Feline immunodeficiency virus
- 1ogk – TcDUTP + dUTP
- 1smc - MtDUTP + dUTP
- 4gcy - MtDUTP (mutant) + dUTP
- 4a6a - MtDUTP (mutant) + dTTP
- 1vyq, 3t60, 3t64, 3t6y, 3t70 - PfDUTP + uridine derivative inhibitor – Plasmodium falciparum
- 2y8c - PfDUTP + trityl ligand
- 2bsy, 2we0 - EbvDUTP + dUMP – Epstein-Barr virus
- 2we1, 2we2 - EbvDUTP (mutant) + dUMP
- 2ol1 - VvDUTP + dUMP
- 2y1t - BsDUTP + dUDP
- 4ao5 - BsDUTP + dUMP
- 2yb0 - LmDUTP + dU – Leishmania major
- 3tq5, 3trl, 3trn, 3ts6, 3tsl, 3tta - MPmvDUTP catalytic domain (mutant) + dUMP
- 4ooq, 2pc5 – AtDUTP + Mg – Arabidopsis thaliana
- 4mz5, 4mz6 – hDUTP + importin subunit α-1
- 5h4j - hDUTP + inhibitor
- 3zf0, 3zf1, 3zf2, 3zf3, 3zf4, 3zf5, 3zf6, 5cct, 5nyz, 5nz2 - SpDUTP (mutant) + dUTP derivative – Staphylococcus phage 80α
- 5cco - SpDUTP + dUMP
- 4gv8 - DUTP + dUTP derivative – Staphylococcus phage 11
- 4wrk - DUTP (mutant) + dUTP derivative – Staphylococcus phage φ11
- 5myd - DUTP + dUTP derivative – Staphylococcus
- DUTP ternary complexes
- 1duc – EvDUPT + Sr + dUTP
- 1six, 1sjn, 2py4 – MtDUTP + Mg + dUTP derivative
- 3h6d, 3hza, 3i93 - MtDUTP (mutant) + Mg + dUTP derivative
- 3loj - MtDUTP (mutant) + Mg + Mn + dUTP derivative
- 1rn8 - EcDUTP + Mg + dUTP derivative
- 1rnj - EcDUTP (mutant) + Mg + dUTP derivative
- 1syl - EcDUTP (mutant) + Mg + dUTP
- 2hr6 - EcDUTP + Mn + dUDP
- 1slh – MtDUTP + Mg + dUDP
- 5ect, 5edd - MtDUTP (mutant) + Mg + dUTP derivative
- 1sm8 – MtDUTP + Cr + dUTP
- 1snf - MtDUTP + Mg + dUMP
- 1w2y, 2cic - DUTP + Mg + dUTP derivative – Campylobacter jejuni
- 5f9k - DUTP + Mg + dUTP derivative – slime mold
- 2bt1 - EbvDUTP + Mg + dUTP derivative
- 2we3 - EbvDUTP residues 1-256 + Mg + dUTP
- 2d4n - MPmvDUTP residues 83-234 (mutant) + Mg + dUTP derivative
- 3tp1 - MPmvDUTP catalytic domain + Mg + dUTP derivative
- 3tpw, 3tpn, 3tps - MPmvDUTP catalytic domain (mutant) + Mg + dUTP derivative
- 3tpy, 3tq3, 3tq4 - MPmvDUTP catalytic domain + Mg + dUMP + dUTP derivative
- 2cje - LmDUTP + Mg + dUTP derivative
- 2yay - LmDUTP + Ca + dUTP derivative
- 2yaz - LmDUTP + Mg + dUMP
- 2oke - VvDUTP + Mg + dUTP derivative
- 2ol0 - VvDUTP + Mg + dUDP
- 3c3i - PbcvDUTP (mutant) + Mg + dUDP – Paramecium bursaria chlorella virus
- 3c2t, 3ca9 - PbcvDUTP + Mg + dUDP
- 2hqu - hDUTP + Mg + dUTP derivative
- 1q5h - hDUTP + Mg + dUDP
- 3ehw - hDUTP + Mg + dUTP
- 3ara, 3arn - hDUTP + Mg + uracil derivative
- 3p48 - yDUTP + Mg + dUTP derivative
- 2xy3 - BsDUTP + Mg + dUTP derivative
- 4oop - AtDUTP + Mg + dUTP derivative
- 4aoo, 4apz, 4aoz - BsDUTP + Mg + PPi + uridine
ReferencesReferences
- ↑ 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
- ↑ 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
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