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Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain.

Abstract:

Dihydroxyacetone kinases are a sequence-conserved family of enzymes, which utilize two different phosphoryldonors, ATP in animals, plants and some bacteria, and a multiphosphoprotein of the phosphoenolpyruvate carbohydrate phosphotransferase system in bacteria. Here we report the 2.5-A crystal structure of the homodimeric Citrobacter freundii dihydroxyacetone kinase complex with an ATP analogue and dihydroxyacetone. The N-terminal domain consists of two alpha/beta-folds with a molecule of dih...

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Publisher copy:
10.1074/jbc.m305942200

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
Journal:
The Journal of biological chemistry
Volume:
278
Issue:
48
Pages:
48236-48244
Publication date:
2003-11-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:196c5a30-593d-465f-81d2-9758cef4961d
Source identifiers:
12289
Local pid:
pubs:12289

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