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2LCA

Solution structure of the C domain of RV0899 from mycobacterium tuberculosis

2LCA の概要
エントリーDOI10.2210/pdb2lca/pdb
分子名称Uncharacterized protein Rv0899/MT0922 (1 entity in total)
機能のキーワードpeptidoglycan-binding protein
由来する生物種Mycobacterium tuberculosis
細胞内の位置Cell membrane; Multi-pass membrane protein (Potential): P65593
タンパク質・核酸の鎖数1
化学式量合計14096.71
構造登録者
Marassi, F.,Yao, Y. (登録日: 2011-04-26, 公開日: 2012-01-04, 最終更新日: 2024-10-30)
主引用文献Yao, Y.,Barghava, N.,Kim, J.,Niederweis, M.,Marassi, F.M.
Molecular Structure and Peptidoglycan Recognition of Mycobacterium tuberculosis ArfA (Rv0899).
J.Mol.Biol., 416:208-220, 2012
Cited by
PubMed Abstract: Mycobacterium tuberculosis ArfA (Rv0899) is a membrane protein encoded by an operon that is required for supporting bacterial growth in acidic environments. Its C-terminal domain (C domain) shares significant sequence homology with the OmpA-like family of peptidoglycan-binding domains, suggesting that its physiological function in acid stress protection may be related to its interaction with the mycobacterial cell wall. Previously, we showed that ArfA forms three independently structured modules, and we reported the structure of its central domain (B domain). Here, we describe the high-resolution structure and dynamics of the C domain, we identify ArfA as a peptidoglycan-binding protein and we elucidate the molecular basis for its specific recognition of diaminopimelate-type peptidoglycan. The C domain of ArfA adopts the characteristic fold of the OmpA-like family. It exhibits pH-dependent conformational dynamics (with significant heterogeneity at neutral pH and a more ordered structure at acidic pH), which could be related to its acid stress response. The C domain associates tightly with polymeric peptidoglycan isolated from M. tuberculosis and also associates with a soluble peptide intermediate of peptidoglycan biosynthesis. This enabled us to characterize the peptidoglycan binding site where five highly conserved ArfA residues, including two key arginines, establish the specificity for diaminopimelate- but not Lys-type peptidoglycan. ArfA is the first peptidoglycan-binding protein to be identified in M. tuberculosis. Its functions in acid stress protection and peptidoglycan binding suggest a link between the acid stress response and the physicochemical properties of the mycobacterial cell wall.
PubMed: 22206986
DOI: 10.1016/j.jmb.2011.12.030
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2lca
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2026-01-28に公開中

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