- Abstract:
-
The crystal structure of the dUTPase from the important gastric pathogen Campylobacter jejuni has been solved at 1.65 A spacing. This essential bacterial enzyme is the second representative of the new family of dimeric dUTPases to be structurally characterised. Members of this family have a novel all-alpha fold and are unrelated to the all-beta dUTPases of the majority of organisms including eukaryotes such as humans, bacteria such as Escherichia coli, archaea like Methanococcus jannaschii an...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/j.jmb.2004.07.050
-
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- Journal:
- Journal of molecular biology
- Volume:
- 342
- Issue:
- 5
- Pages:
- 1583-1597
- Publication date:
- 2004-10-05
- DOI:
- EISSN:
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1089-8638
- ISSN:
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0022-2836
- URN:
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uuid:f91fd818-5296-422e-8752-96f4776243a2
- Source identifiers:
-
32842
- Local pid:
- pubs:32842
- Copyright date:
- 2004
Journal article
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.
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