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X‐ray crystal structure of the B component of Hemolysin BL from Bacillus cereus
Author(s) -
Madegowda Mahendra,
Eswaramoorthy Subramaniam,
Burley Stephen K.,
Swaminathan Subramanyam
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21888
Subject(s) - bacillus cereus , hemolysin , enterotoxin , virulence , cereus , microbiology and biotechnology , ternary complex , chemistry , biology , crystallography , biochemistry , bacteria , genetics , escherichia coli , gene , enzyme
Bacillus cereus Hemolysin BL enterotoxin, a ternary complex of three proteins, is the causative agent of food poisoning and requires all three components for virulence. The X‐ray structure of the binding domain of HBL suggests that it may form a pore similar to other soluble channel forming proteins. A putative pathway of pore formation is discussed. Proteins 2008; 71:534–540. Published 2007 Wiley‐Liss, Inc.