5IMY

Trapped Toxin

Summary for 5IMY

• Entry DOI: 10.2210/pdb5imy/pdb
• Descriptor: Vaginolysin, CD59 glycoprotein (3 entities in total)
• Functional Keywords: toxin-toxin receptor complex, toxin/toxin receptor
• Biological source: Gardnerella vaginalis; More
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor: P13987
• Total number of polymer chains: 4
• Total formula weight: 126629.34

Authors

Lawrence, S.L.,Morton, C.J.,Parker, M.W. (deposition date: 2016-03-07, release date: 2016-08-24, Last modification date: 2024-11-06)

Primary citation

Lawrence, S.L.,Gorman, M.A.,Feil, S.C.,Mulhern, T.D.,Kuiper, M.J.,Ratner, A.J.,Tweten, R.K.,Morton, C.J.,Parker, M.W.
Structural Basis for Receptor Recognition by the Human CD59-Responsive Cholesterol-Dependent Cytolysins.
Structure, 24:1488-1498, 2016

PubMed Abstract: Cholesterol-dependent cytolysins (CDCs) are a family of pore-forming toxins that punch holes in the outer membrane of eukaryotic cells. Cholesterol serves as the receptor, but a subclass of CDCs first binds to human CD59. Here we describe the crystal structures of vaginolysin and intermedilysin complexed to CD59. These studies, together with small-angle X-ray scattering, reveal that CD59 binds to each at different, though overlapping, sites, consistent with molecular dynamics simulations and binding studies. The CDC consensus undecapeptide motif, which for the CD59-responsive CDCs has a proline instead of a tryptophan in the motif, adopts a strikingly different conformation between the structures; our data suggest that the proline acts as a selectivity switch to ensure CD59-dependent CDCs bind their protein receptor first in preference to cholesterol. The structural data suggest a detailed model of how these water-soluble toxins assemble as prepores on the cell surface.

PubMed: 27499440
DOI: 10.1016/j.str.2016.06.017

Experimental method

X-RAY DIFFRACTION (2.4 Å)