| Literature DB >> 29331609 |
Trevor Gokey1, Andrei S Halavaty2, George Minasov2, Wayne F Anderson2, Misty L Kuhn3.
Abstract
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.Entities:
Keywords: Cell wall polysaccharide producing enzymes; Co-crystallization of metabolic enzymes; Dehydratase; Protein crystallization; Therapeutic drug target
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Year: 2018 PMID: 29331609 PMCID: PMC5864537 DOI: 10.1016/j.jsb.2018.01.006
Source DB: PubMed Journal: J Struct Biol ISSN: 1047-8477 Impact factor: 2.867