Get access
Advertisement

Crystal structure of decaprenylphosphoryl-β- D-ribose 2'-epimerase from Mycobacterium smegmatis

Authors

  • Hua Li,

    1. Department of Molecular Biology, Cellular Biology and Biochemistry, Brown University, Providence, Rhode Island 02912
    Search for more papers by this author
  • Gerwald Jogl

    Corresponding author
    1. Department of Molecular Biology, Cellular Biology and Biochemistry, Brown University, Providence, Rhode Island 02912
    • Department of Molecular Biology, Cell Biology and Biochemistry, Box G-E128, Brown University, Providence, RI 02912
    Search for more papers by this author

  • Hua Li's current address is Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390

Abstract

Decaprenylphosphoryl-β-D-ribose 2'-epimerase (DprE1) is an essential enzyme in the biosynthesis of cell wall components and a target for development of anti-tuberculosis drugs. We determined the crystal structure of a truncated form of DprE1 from Mycobacterium smegmatis in two crystal forms to up to 2.35 Å resolution. The structure extends from residue 75 to the C-terminus and shares homology with FAD-dependent oxidoreductases of the vanillyl-alcohol oxidase family including the DprE1 homologue from M. tuberculosis. The M. smegmatis DprE1 structure reported here provides further insights into the active site geometry of this tuberculosis drug target. Proteins 2013. © 2012 Wiley Periodicals, Inc.

Get access to the full text of this article

Ancillary