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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.

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...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2004.07.050

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Institution:
University of Oxford
Department:
Oxford, MSD, Structural Biology
Role:
Author
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Journal:
Journal of molecular biology
Volume:
342
Issue:
5
Pages:
1583-1597
Publication date:
2004-10-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:f91fd818-5296-422e-8752-96f4776243a2
Source identifiers:
32842
Local pid:
pubs:32842

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