2nrj

Crystal Structure of Hemolysin binding component from Bacillus cereusCrystal Structure of Hemolysin binding component from Bacillus cereus

Structural highlights 2nrj is a 1 chain structure with sequence from Bacillus cereus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.03Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemolysin 3D structures

spinqualitylabelsall models 2nrj, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image