Article thumbnail
Location of Repository

Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 angstrom resolution suggests a mechanism for stereocontrol during catalysis

By 

Abstract

Diaminopimelate (DAP) epimerase (DapF) is central to the biosynthesis of both lysine and cell-wall peptidoglycan in many bacteria species. The peptidoglycan layer provides great potential for the development of novel antimicrobials as it is a uniquely prokaryotic feature. Crystals of recombinant Haemophilus influenzae DapF that diffract to beyond 2 Angstrom resolution have been obtained which facilitated the solution of the structure by molecular replacement at a resolution approximately 1 Angstrom higher than that previously determined. An analysis of the structure (i) in comparison to other PLP-independent racemaces and (ii) in relation to the catalytic mechanism and stereospecificity of DapF is presented

Topics: QD, QH301
Publisher: BLACKWELL MUNKSGAARD
OAI identifier: oai:wrap.warwick.ac.uk:8859
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • http://dx.doi.org/10.1107/S090... (external link)
  • Suggested articles


    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.