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Crystal structure of decaprenylphosphoryl‐β‐ D ‐ribose 2'‐epimerase from Mycobacterium smegmatis
Author(s) -
Li Hua,
Jogl Gerwald
Publication year - 2013
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24220
Subject(s) - mycobacterium smegmatis , mycobacterium tuberculosis , stereochemistry , biosynthesis , chemistry , ribose , biochemistry , enzyme , biology , tuberculosis , medicine , pathology
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.