3FVE
Crystal structure of diaminopimelate epimerase Mycobacterium tuberculosis DapF
Summary for 3FVE
| Entry DOI | 10.2210/pdb3fve/pdb |
| Descriptor | Diaminopimelate epimerase, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | alpha/beta, amino-acid biosynthesis, isomerase, lysine biosynthesis |
| Biological source | Mycobacterium tuberculosis |
| Cellular location | Cytoplasm (By similarity): P63897 |
| Total number of polymer chains | 1 |
| Total formula weight | 30203.07 |
| Authors | Usha, V.,Dover, L.G.,Roper, D.I.,Futterer, K.,Besra, G.S. (deposition date: 2009-01-15, release date: 2009-01-27, Last modification date: 2023-09-06) |
| Primary citation | Usha, V.,Dover, L.G.,Roper, D.I.,Futterer, K.,Besra, G.S. Structure of the diaminopimelate epimerase DapF from Mycobacterium tuberculosis Acta Crystallogr.,Sect.D, 65:383-387, 2009 Cited by PubMed Abstract: 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 A 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 ( DOI: 10.1107/S0907444909002522 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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