5IMT: Toxin receptor complex

Citation:
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.
PDB ID: 5IMTDownload
MMDB ID: 142276
PDB Deposition Date: 2016/3/6
Updated in MMDB: 2016/09
Experimental Method:
x-ray diffraction
Resolution: 2.7001  Å
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 5IMT: tetrameric; determined by author and by software (PISA)
Molecular Components in 5IMT
Label Count Molecule
Proteins (4 molecules)
2
Intermedilysin
Molecule annotation
2
Cd59 Glycoprotein(Gene symbol: CD59)
Molecule annotation
Chemicals (26 molecules)
1
2
2
6
3
14
4
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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