Structure of the Bacillus anthracis dTDP-L-rhamnose biosynthetic pathway enzyme: dTDP-α-D-glucose 4,6-dehydratase, RfbB

Trevor Gokey, Andrei S. Halavaty, George Minasov, Wayne F. Anderson, Misty L. Kuhn*

*Corresponding author for this work

Research output: Contribution to journalArticle

1 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)175-181
Number of pages7
JournalJournal of Structural Biology
Volume202
Issue number2
DOIs
StatePublished - May 2018

Keywords

  • Cell wall polysaccharide producing enzymes
  • Co-crystallization of metabolic enzymes
  • Dehydratase
  • Protein crystallization
  • Therapeutic drug target

ASJC Scopus subject areas

  • Structural Biology

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