2MKX: Solution structure of LysM the peptidoglycan binding domain of autolysin AtlA from Enterococcus faecalis

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.
PDB ID: 2MKXDownload
MMDB ID: 120711
PDB Deposition Date: 2014/2/14
Updated in MMDB: 2014/07
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2MKX: monomeric; determined by author
Molecular Components in 2MKX
Label Count Molecule
Protein (1 molecule)
Autolysin(Gene symbol: EF0799)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB