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Structure of the Bacillus anthracis dTDP-l-rhamnose biosynthetic pathway enzyme: dTDP-α-d-glucose 4,6-dehydratase, RfbB.

Authors
  • Gokey, Trevor1
  • Halavaty, Andrei S2
  • Minasov, George2
  • Anderson, Wayne F2
  • Kuhn, Misty L3
  • 1 Department of Chemistry and Biochemistry, San Francisco State University, USA.
  • 2 Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, USA; Center for Structural Genomics of Infectious Diseases (CSGID), USA.
  • 3 Department of Chemistry and Biochemistry, San Francisco State University, USA. Electronic address: [email protected]
Type
Published Article
Journal
Journal of Structural Biology
Publisher
Elsevier
Publication Date
May 01, 2018
Volume
202
Issue
2
Pages
175–181
Identifiers
DOI: 10.1016/j.jsb.2018.01.006
PMID: 29331609
Source
Medline
Keywords
Language
English
License
Unknown

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. Copyright © 2018 Elsevier Inc. All rights reserved.

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