Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8648211 | Journal of Structural Biology | 2018 | 7 Pages |
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.
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Authors
Trevor Gokey, Andrei S. Halavaty, George Minasov, Wayne F. Anderson, Misty L. Kuhn,