short communications
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 Å resolution have been obtained which facilitated the solution of the structure by molecular replacement at a resolution approximately 1 Å 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.
Supporting information
Portable Document Format (PDF) file https://doi.org/10.1107/S0907444903027999/hv5003sup1.pdf |
PDB reference: diaminopimelate epimerase, 1gqz, r1gqzsf