Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 angstrom resolution suggests a mechanism for stereocontrol during catalysis
UNSPECIFIED. (2004) Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 angstrom resolution suggests a mechanism for stereocontrol during catalysis. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 60 (Part 2). pp. 397-400. ISSN 0907-4449Full text not available from this repository.
Official URL: http://dx.doi.org/10.1107/S0907444903027999
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.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY|
|Official Date:||February 2004|
|Number of Pages:||4|
|Page Range:||pp. 397-400|
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