Molecular basis for bacterial peptidoglycan recognition by LysM domains

Stéphane Mesnage, Mariano Dellarole, Nicola J. Baxter, Jean Baptiste Rouget, Jordan D. Dimitrov, Ning Wang, Yukari Fujimoto, Andrea M. Hounslow, Sébastien Lacroix-Desmazes, Koichi Fukase, Simon J. Foster, Michael P. Williamson

研究成果: Article査読

115 被引用数 (Scopus)

抄録

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.

本文言語English
論文番号4269
ジャーナルNature communications
5
DOI
出版ステータスPublished - 2014 6月 30
外部発表はい

ASJC Scopus subject areas

  • 化学 (全般)
  • 生化学、遺伝学、分子生物学(全般)
  • 物理学および天文学(全般)

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