2nrj

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

Structural highlights

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

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

  1. 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

2nrj, resolution 2.03Å

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