3HVN

Crystal structure of cytotoxin protein suilysin from Streptococcus suis

Summary for 3HVN

• Entry DOI: 10.2210/pdb3hvn/pdb
• Descriptor: Hemolysin, 1,1,1,3,3,3-hexafluoropropan-2-ol, HEPTANE-1,2,3-TRIOL, ... (4 entities in total)
• Functional Keywords: beta-strand rich, elongated rod like, pore forming, toxin
• Biological source: Streptococcus suis
• Total number of polymer chains: 1
• Total formula weight: 56417.46

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 citation

Xu, 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

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

Experimental method

X-RAY DIFFRACTION (2.852 Å)