3FVE
Crystal structure of diaminopimelate epimerase Mycobacterium tuberculosis DapF
3FVE の概要
| エントリーDOI | 10.2210/pdb3fve/pdb |
| 分子名称 | Diaminopimelate epimerase, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, GLYCEROL, ... (4 entities in total) |
| 機能のキーワード | alpha/beta, amino-acid biosynthesis, isomerase, lysine biosynthesis |
| 由来する生物種 | Mycobacterium tuberculosis |
| 細胞内の位置 | Cytoplasm (By similarity): P63897 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 30203.07 |
| 構造登録者 | Usha, V.,Dover, L.G.,Roper, D.I.,Futterer, K.,Besra, G.S. (登録日: 2009-01-15, 公開日: 2009-01-27, 最終更新日: 2023-09-06) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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