2MKX

Solution structure of LysM the peptidoglycan binding domain of autolysin AtlA from Enterococcus faecalis

2MKX の概要

• エントリーDOI: 10.2210/pdb2mkx/pdb
• NMR情報: BMRB: 19799
• 分子名称: Autolysin (1 entity in total)
• 機能のキーワード: protein, hydrolase
• 由来する生物種: Enterococcus faecalis
• 細胞内の位置: Secreted (Probable): P37710
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6400.25

構造登録者

Baxter, N.J.,Williamson, M.P. (登録日: 2014-02-14, 公開日: 2014-06-18, 最終更新日: 2024-05-15)

主引用文献

Mesnage, S.,Dellarole, M.,Baxter, N.J.,Rouget, J.B.,Dimitrov, J.D.,Wang, N.,Fujimoto, Y.,Hounslow, A.M.,Lacroix-Desmazes, S.,Fukase, K.,Foster, S.J.,Williamson, M.P.
Molecular basis for bacterial peptidoglycan recognition by LysM domains.
Nat Commun, 5:4269-4269, 2014

PubMed Abstract: Carbohydrate recognition is essential for growth, cell adhesion and signalling in all living organisms. A highly conserved carbohydrate binding module, LysM, is found in proteins from viruses, bacteria, fungi, plants and mammals. LysM modules recognize polysaccharides containing N-acetylglucosamine (GlcNAc) residues including peptidoglycan, an essential component of the bacterial cell wall. However, the molecular mechanism underpinning LysM-peptidoglycan interactions remains unclear. Here we describe the molecular basis for peptidoglycan recognition by a multimodular LysM domain from AtlA, an autolysin involved in cell division in the opportunistic bacterial pathogen Enterococcus faecalis. We explore the contribution of individual modules to the binding, identify the peptidoglycan motif recognized, determine the structures of free and bound modules and reveal the residues involved in binding. Our results suggest that peptide stems modulate LysM binding to peptidoglycan. Using these results, we reveal how the LysM module recognizes the GlcNAc-X-GlcNAc motif present in polysaccharides across kingdoms.

PubMed: 24978025
DOI: 10.1038/ncomms5269

実験手法

SOLUTION NMR