3LEI: Lectin Domain Of Lectinolysin Complexed With Fucose

The cholesterol-dependent cytolysins (CDCs) punch holes in target cell membranes through a highly regulated process. Streptococcus mitis lectinolysin (LLY) exhibits another layer of regulation with a lectin domain that enhances the pore-forming activity of the toxin. We have determined the crystal structures of the lectin domain by itself and in complex with various glycans that reveal the molecular basis for the Lewis antigen specificity of LLY. A small-angle X-ray scattering study of intact LLY reveals the molecule is flat and elongated with the lectin domain oriented so that the Lewis antigen-binding site is exposed. We suggest that the lectin domain enhances the pore-forming activity of LLY by concentrating toxin molecules at fucose-rich sites on membranes, thus promoting the formation of prepore oligomers on the surface of susceptible cells.
PDB ID: 3LEIDownload
MMDB ID: 87592
PDB Deposition Date: 2010/1/14
Updated in MMDB: 2010/12
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 3LEI: monomeric; determined by author and by software (PISA)
Molecular Components in 3LEI
Label Count Molecule
Protein (1 molecule)
Platelet Aggregation Factor Sm-hpaf
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

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