Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 angstrom resolution suggests a mechanism for stereocontrol during catalysis
- Author(s)
- Lloyd, AJ; Huyton, T; Turkenburg, J; Roper, DI;
- Journal Title
- ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Publication Type
- Journal Article
- 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.
- Publisher
- BLACKWELL MUNKSGAARD
- Keywords
- ESCHERICHIA-COLI; MACROMOLECULAR STRUCTURES; GLUTAMATE RACEMASE; PURIFICATION; EXPRESSION
- Publisher's Version
- https://doi.org/10.1107/S0907444903027999
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2004-02-01 12:00:00