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3FVE

Crystal structure of diaminopimelate epimerase Mycobacterium tuberculosis DapF

3FVE の概要
エントリーDOI10.2210/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 (PubMed: 19307721
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)
構造検証レポート
Validation report summary of 3fve
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-07-01に公開中

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