1S3R

Crystal structure of the human-specific toxin intermedilysin

Summary for 1S3R

• Entry DOI: 10.2210/pdb1s3r/pdb
• Descriptor: intermedilysin, SULFATE ION (3 entities in total)
• Functional Keywords: toxin
• Biological source: Streptococcus intermedius
• Total number of polymer chains: 2
• Total formula weight: 118514.00

Authors

Polekhina, G.,Giddings, K.S.,Tweten, R.K.,Parker, M.W. (deposition date: 2004-01-14, release date: 2005-01-25, Last modification date: 2024-03-13)

Primary citation

Polekhina, G.,Giddings, K.S.,Tweten, R.K.,Parker, M.W.
Insights into the action of the superfamily of cholesterol-dependent cytolysins from studies of intermedilysin
Proc.Natl.Acad.Sci.Usa, 102:600-605, 2005

PubMed Abstract: The cholesterol-dependent cytolysins (CDCs), a superfamily of pore-forming toxins, are characterized by a conserved undecapeptide motif that is believed to be critical for membrane recognition by means of cholesterol. Intermedilysin (ILY), an unusual member of the CDCs, exhibits specificity for human cells and contains nonconservative substitutions in the motif. We show that the cellular specificity of ILY is based on its ability to specifically bind to human cells and does not involve some other feature of the CDC mechanism. Furthermore, cellular recognition by ILY appears to be encoded in domain 4 alone but does not involve the variant undecapeptide of ILY. We show that the undecapeptide is involved in the prepore-to-pore conversion of ILY and so demonstrate a direct connection between the structure of the undecapeptide and the prepore-to-pore transition. We have determined the crystal structure of ILY, which, when compared to the known structure of a prototypical CDC, suggests that the basic aspects of its 3D structure are likely to be conserved in all CDCs.

PubMed: 15637162
DOI: 10.1073/pnas.0403229101

Experimental method

X-RAY DIFFRACTION (2.6 Å)