- 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...
Expand abstract - Publisher copy:
- 10.1074/jbc.m305942200
-
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- Journal:
- The Journal of biological chemistry
- Volume:
- 278
- Issue:
- 48
- Pages:
- 48236-48244
- Publication date:
- 2003-11-05
- DOI:
- EISSN:
-
1083-351X
- ISSN:
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0021-9258
- URN:
-
uuid:196c5a30-593d-465f-81d2-9758cef4961d
- Source identifiers:
-
12289
- Local pid:
- pubs:12289
- Language:
- English
- Keywords:
- Copyright date:
- 2003
Journal article
Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain.
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