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3HVN

Crystal structure of cytotoxin protein suilysin from Streptococcus suis

Summary for 3HVN
Entry DOI10.2210/pdb3hvn/pdb
DescriptorHemolysin, 1,1,1,3,3,3-hexafluoropropan-2-ol, HEPTANE-1,2,3-TRIOL, ... (4 entities in total)
Functional Keywordsbeta-strand rich, elongated rod like, pore forming, toxin
Biological sourceStreptococcus suis
Total number of polymer chains1
Total formula weight56417.46
Authors
Xu, L.,Huang, B.,Du, H.,Zhang, C.X.,Xu, J.,Li, X.,Rao, Z. (deposition date: 2009-06-16, release date: 2010-03-02, Last modification date: 2024-05-29)
Primary citationXu, L.,Huang, B.,Du, H.,Zhang, X.C.,Xu, J.,Li, X.,Rao, Z.
Crystal structure of cytotoxin protein suilysin from Streptococcus suis.
Protein Cell, 1:96-105, 2010
Cited by
PubMed Abstract: Cholesterol-dependent cytolysins (CDC) are pore forming toxins. A prototype of the CDC family members is perfringolysin O (PFO), which directly binds to the cell membrane enriched in cholesterol, causing cell lysis. However, an exception of this general observation is intermedilysin (ILY) of Streptococcus intermedius, which requires human CD59 as a receptor in addition to cholesterol for its hemolytic activity. A possible explanation of this functional difference is the conformational variation between the C-terminal domains of the two toxins, particularly in the highly conserved undecapeptide termed tryptophan rich motif. Here, we present the crystal structure of suilysin, a CDC toxin from the infectious swine pathogen Streptococcus suis. Like PFO, suilysin does not require a host receptor for hemolytic activity; yet the crystal structure of suilysin exhibits a similar conformation in the tryptophan rich motif to ILY. This observation suggests that the current view of the structure-function relationship between CDC proteins and membrane association is far from complete.
PubMed: 21204001
DOI: 10.1007/s13238-010-0012-3
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.852 Å)
Structure validation

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