title: Molecular basis for bacterial peptidoglycan recognition by LysM domains.
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.
authors: 1] Krebs Institute, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK [2] Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
authors: Stéphane
authors: S
authors: Mesnage
authors: 1] Centre de Biochimie Structurale, CNRS UMR 5048-UM 1-INSERM UMR 1054, F-34090 Montpellier, France [2] [3].
authors: Mariano
authors: M
authors: Dellarole
authors: 1] Krebs Institute, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK [2] Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK [3].
authors: Nicola J
authors: NJ
authors: Baxter
authors: Centre de Biochimie Structurale, CNRS UMR 5048-UM 1-INSERM UMR 1054, F-34090 Montpellier, France.
authors: Jean-Baptiste
authors: JB
authors: Rouget
authors: 1] INSERM, U872, Centre de Recherche des Cordeliers, Equipe 16, F-75006 Paris, France [2] Université Pierre et Marie Curie, UMR-S 872, F-75006 Paris, France [3] Université Paris Descartes, UMR-S 872, F-75006 Paris, France.
authors: Jordan D
authors: JD
authors: Dimitrov
authors: Department of Chemistry, Laboratory for Natural Products Chemistry, Osaka University, Osaka 560-0043, Japan.
authors: Ning
authors: N
authors: Wang
authors: Department of Chemistry, Laboratory for Natural Products Chemistry, Osaka University, Osaka 560-0043, Japan.
authors: Yukari
authors: Y
authors: Fujimoto
authors: 1] Krebs Institute, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK [2] Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
authors: Andrea M
authors: AM
authors: Hounslow
authors: 1] INSERM, U872, Centre de Recherche des Cordeliers, Equipe 16, F-75006 Paris, France [2] Université Pierre et Marie Curie, UMR-S 872, F-75006 Paris, France [3] Université Paris Descartes, UMR-S 872, F-75006 Paris, France.
authors: Sébastien
authors: S
authors: Lacroix-Desmazes
authors: Department of Chemistry, Laboratory for Natural Products Chemistry, Osaka University, Osaka 560-0043, Japan.
authors: Koichi
authors: K
authors: Fukase
authors: 1] Krebs Institute, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK [2] Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
authors: Simon J
authors: SJ
authors: Foster
authors: 1] Krebs Institute, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK [2] Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK.
authors: Michael P
authors: MP
authors: Williamson
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D013293:Enterococcus faecalis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D010457:Peptidoglycan / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins; D010457:Peptidoglycan