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

Authors
  • Li, Hua
  • Jogl, Gerwald
Type
Published Article
Journal
Proteins Structure Function and Bioinformatics
Publisher
Wiley (John Wiley & Sons)
Publication Date
Mar 01, 2013
Volume
81
Issue
3
Pages
538–543
Identifiers
DOI: 10.1002/prot.24220
PMID: 23184707
Source
Medline
License
Unknown

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.

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