Structural highlights
Function
HBLA_BACCE Cytotoxic protein, part of the enterotoxin complex. Responsible for binding to erythrocytes. This enterotoxin is thought to be the cause of the diarrheal form of gastroenteritis caused by food-borne strains of B.cereus.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
X-ray crystal structure of the B component of Hemolysin BL from Bacillus cereus.,Madegowda M, Eswaramoorthy S, Burley SK, Swaminathan S Proteins. 2008 May 1;71(2):534-40. PMID:18175317[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Madegowda M, Eswaramoorthy S, Burley SK, Swaminathan S. X-ray crystal structure of the B component of Hemolysin BL from Bacillus cereus. Proteins. 2008 May 1;71(2):534-40. PMID:18175317 doi:10.1002/prot.21888
