Structure of the diaminopimelate epimerase DapF from Mycobacterium tuberculosis

V Usha, LG Dover, DI Roper, Klaus Futterer, Gurdyal Besra

Research output: Contribution to journalArticle

16 Citations (Scopus)


The meso (or d,L) isomer of diaminopimelic acid (DAP), a precursor of L-lysine, is a key component of the pentapeptide linker in bacterial peptidoglycan. While the peptidoglycan incorporated in the highly complex cell wall of the pathogen Mycobacterium tuberculosis structurally resembles that of Escherichia coli, it is unique in that it can contain penicillin-resistant meso-DAP -> meso-DAP linkages. The interconversion of L,L-DAP and meso-DAP is catalysed by the DAP epimerase DapF, a gene product that is essential in M. tuberculosis. Here, the crystal structure of the ligand-free form of M. tuberculosis DapF (MtDapF) refined to a resolution of 2.6 angstrom is reported. MtDapF shows small if distinct deviations in secondary structure from the two-domain alpha/beta-fold of the known structures of Haemophilus influenzae DapF and Bacillus anthracis DapF, which are in line with its low sequence identity (
Original languageEnglish
Pages (from-to)383-387
Number of pages5
JournalActa Crystallographica Section D Biological Crystallography
Issue number4
Publication statusPublished - 1 Apr 2009


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