3LEG

Lectin Domain of Lectinolysin complexed with Lewis Y Antigen

Summary for 3LEG

• Entry DOI: 10.2210/pdb3leg/pdb
• Related: 3LEI 3LEK 3LEO
• Related PRD ID: PRD_900054
• Descriptor: Platelet aggregation factor Sm-hPAF, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: lectin domain of lectinolysin, lewis y antigen, blood clotting, nickel
• Biological source: Streptococcus mitis
• Total number of polymer chains: 1
• Total formula weight: 17641.88

Authors

Feil, S.C. (deposition date: 2010-01-14, release date: 2010-12-29, Last modification date: 2023-09-06)

Primary citation

Feil, S.C.,Lawrence, S.,Mulhern, T.D.,Holien, J.K.,Hotze, E.M.,Farrand, S.,Tweten, R.K.,Parker, M.W.
Structure of the lectin regulatory domain of the cholesterol-dependent cytolysin lectinolysin reveals the basis for its lewis antigen specificity.
Structure, 20:248-258, 2012

PubMed Abstract: 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.

PubMed: 22325774
DOI: 10.1016/j.str.2011.11.017

Experimental method

X-RAY DIFFRACTION (2.01 Å)