2NRJ
Crystal Structure of Hemolysin binding component from Bacillus cereus
Summary for 2NRJ
Entry DOI | 10.2210/pdb2nrj/pdb |
Descriptor | Hbl B protein (2 entities in total) |
Functional Keywords | enterotoxin; hemolysis; transmembrane, structural genomics, psi-2, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, toxin |
Biological source | Bacillus cereus |
Total number of polymer chains | 1 |
Total formula weight | 38934.70 |
Authors | Madegowda, M.,Eswaramoorthy, S.,Burley, S.K.,Swaminathan, S.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2006-11-02, release date: 2006-11-14, Last modification date: 2024-10-30) |
Primary citation | Madegowda, M.,Eswaramoorthy, S.,Burley, S.K.,Swaminathan, S. X-ray crystal structure of the B component of Hemolysin BL from Bacillus cereus Proteins, 71:534-540, 2008 Cited by PubMed Abstract: 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. PubMed: 18175317DOI: 10.1002/prot.21888 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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