Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 A resolution suggests a mechanism for stereocontrol during catalysis.
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 A resolution have been obtained which facilitated the solution of the structure by molecular replacement at a resolution approximately 1 A 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.
Lloyd
Adrian John
AJ
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, England.
Huyton
Trevor
T
Turkenburg
Johan
J
Roper
David Ian
DI
D000591:Amino Acid Isomerases / Q000737:chemistry*; D002384:Catalysis; D002473:Cell Wall; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D006193:Haemophilus influenzae / Q000378:metabolism*; D008239:Lysine / Q000737:chemistry; D008956:Models, Chemical; D008958:Models, Molecular; D010457:Peptidoglycan / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry
D010457:Peptidoglycan; D011994:Recombinant Proteins; D000591:Amino Acid Isomerases; C042032:diaminopimelate epimerase; D008239:Lysine