![]() |
|
PROSITE documentation PDOC51782 |
A highly conserved carbohydrate binding module, LysM (lysin-like motif), is found in proteins from viruses, bacteria, fungi, plants and mammals. It is present in bacterial extracellular proteins including hydrolases, adhesins and virulence factors such as Protein A from Staphylococcus aureus. It is also found in proteins produced by fungal pathogens acting as modulators of host immunity, and is present in a large number of proteins from insects, mammals and plants involved in defence against pathogens and symbiotic signalling. LysM modules recognize polysaccharides containing N-acetylglucosamine (GlcNAc) residues including peptidoglycan, an essential component of the bacterial cell wall. Prokaryotic LysM modules bind peptidoglycan, the main component of the bacterial cell wall, made of alternating N-acetylglycosamine (GlcNac) and N-acetylmuramic acid (MurNac) residues, substituted by short peptide stems. In eukaryotes, LysM domains have been shown to bind mainly to chitin, a β 1,4-linked GlcNac polymer that is the main constituent of fungal cell walls, as well as to peptidoglycan [1,2].
LysM modules consist of 43-50 amino acids that adopt a highly conserved βααβ-fold, with the two helices packing onto the same side of a two stranded anti-parallel β-sheet (see <PDB:1E0G>). The sequence conservation is particularly high in the first 16 residues [1,2].
Some proteins known to contain a LysM domain are listed below:
The profile we developed covers the entire LysM domain.
Last update:November 2015 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Bateman A. Bycroft M. |
Title | The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). | |
Source | J. Mol. Biol. 299:1113-1119(2000). | |
PubMed ID | 10843862 | |
DOI | 10.1006/jmbi.2000.3778 |
2 | Authors | 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. |
Title | Molecular basis for bacterial peptidoglycan recognition by LysM domains. | |
Source | Nat. Commun. 5:4269-4269(2014). | |
PubMed ID | 24978025 | |
DOI | 10.1038/ncomms5269 |