Structural highlights
Publication Abstract from PubMed
Decaprenylphosphoryl-beta-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 A 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.
Crystal structure of decaprenylphosphoryl-beta- D-ribose 2'-epimerase from Mycobacterium smegmatis.,Li H, Jogl G Proteins. 2013 Mar;81(3):538-43. doi: 10.1002/prot.24220. Epub 2012 Dec 24. PMID:23184707[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li H, Jogl G. Crystal structure of decaprenylphosphoryl-beta- D-ribose 2'-epimerase from Mycobacterium smegmatis. Proteins. 2013 Mar;81(3):538-43. doi: 10.1002/prot.24220. Epub 2012 Dec 24. PMID:23184707 doi:10.1002/prot.24220
