Bacillus thuringiensis cytolytic toxin associates specifically with its synthetic helices A and C in the membrane bound state. Implications for the assembly of oligomeric transmembrane pores

Biochemistry

Volumn 36, Issue 49, 1997, Pages 15546-15554

  Gazit, Ehud ^a   Burshtein, Noga ^a   Ellar, David J ^b   Sawyer, Trevor ^b   Shai, Yechiel ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; OLIGOMER; SYNTHETIC PEPTIDE;

ALPHA HELIX; ARTICLE; BACILLUS THURINGIENSIS; CELL MEMBRANE; CHANNEL GATING; CONTROLLED STUDY; CYTOLYSIS; LIPID MEMBRANE; MEMBRANE BINDING; MEMBRANE TRANSPORT; MOLECULAR INTERACTION; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY;

AMINO ACID SEQUENCE; BACILLUS THURINGIENSIS; BACTERIAL PROTEINS; BACTERIAL TOXINS; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CIRCULAR DICHROISM; ENDOTOXINS; HEMOLYSIN PROTEINS; HEMOLYSIS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; SEQUENCE HOMOLOGY, AMINO ACID; X-RAY DIFFRACTION;

BACILLUS THURINGIENSIS; BACTERIA (MICROORGANISMS);

EID: 0030708560     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9707584     Document Type: Article

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