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Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 angstrom resolution suggests a mechanism for stereocontrol during catalysis
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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 0907-4449
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Official URL: http://dx.doi.org/10.1107/S0907444903027999
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.
| 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 |
| Publisher: | BLACKWELL MUNKSGAARD |
| ISSN: | 0907-4449 |
| Date: | February 2004 |
| Volume: | 60 |
| Number: | Part 2 |
| Number of Pages: | 4 |
| Page Range: | pp. 397-400 |
| Identification Number: | 10.1107/S0907444903027999 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/8859 |
Data sourced from Thomson Reuters' Web of Knowledge
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