Structure of the Bacillus anthracis dTDP- l -rhamnose biosynthetic pathway enzyme: dTDP-α- d -glucose 4,6-dehydratase, RfbB
| Autor: | Trevor Gokey, Andrei S. Halavaty, George Minasov, Wayne F. Anderson, Misty L. Kuhn |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Protein Conformation Crystallography X-Ray Article Cell wall 03 medical and health sciences chemistry.chemical_compound Structural Biology D-Glucose Thymine Nucleotides Hydro-Lyases chemistry.chemical_classification 030102 biochemistry & molecular biology biology Nucleoside Diphosphate Sugars biology.organism_classification Biosynthetic Pathways Bacillus anthracis 030104 developmental biology Enzyme chemistry Biochemistry DTDP-L-rhamnose Dehydratase Carbohydrate Epimerases Bacteria |
| Zdroj: | Journal of Structural Biology. 202:175-181 |
| ISSN: | 1047-8477 |
| Popis: | Many bacteria require L-rhamnose as a key cell wall component. This sugar is transferred to the cell wall using an activated donor dTDP-L-rhamnose, which is produced by the dTDP-L-rhamnose biosynthetic pathway. We determined the crystal structure of the second enzyme of this pathway dTDP-α-D-glucose 4,6-dehydratase (RfbB) from Bacillus anthracis. Interestingly, RfbB only crystallized in the presence of the third enzyme of the pathway RfbC; however, RfbC was not present in the crystal. Our work represents the first complete structural characterization of the four proteins of this pathway in a single Gram-positive bacterium. |
| Databáze: | OpenAIRE |
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