title: Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 A resolution suggests a mechanism for stereocontrol during catalysis.
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 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.
authors.affiliation: Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, England.
authors.forename: Adrian John
authors.initials: AJ
authors.lastname: Lloyd
authors.forename: Trevor
authors.initials: T
authors.lastname: Huyton
authors.forename: Johan
authors.initials: J
authors.lastname: Turkenburg
authors.forename: David Ian
authors.initials: DI
authors.lastname: Roper
mesh_terms: 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
chemical_list: D010457:Peptidoglycan; D011994:Recombinant Proteins; D000591:Amino Acid Isomerases; C042032:diaminopimelate epimerase; D008239:Lysine