Penetrating insights into pore formation

Penetrating insights into pore formation

Two recent crystal structures show channel-forming bacterial toxins as soluble monomers (colicin la) or transmembrane pores (α-haemolysin). Together with other data, these structures imply that toxin activity requires dramatic conformational changes.

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Bibliographische Detailangaben
Veröffentlicht in:Nature Structural Biology 1997-02, Vol.4 (2), p.89-92
1. Verfasser: Hughson, Frederick M
Format: Artikel
Sprache:eng
Schlagworte:
Bacterial Proteins - chemistry
Bacterial Proteins - toxicity
Bacterial Toxins - chemistry
Binding Sites
Biochemistry
Biological Microscopy
Biomedical and Life Sciences
Colicins - chemistry
Colicins - toxicity
Escherichia coli Proteins
Hemolysin Proteins - chemistry
Hemolysin Proteins - toxicity
Ion Channels
Life Sciences
Membrane Biology
Models, Structural
news-and-views
Protein Conformation
Protein Structure
Protein Structure, Secondary
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Beschreibung
Zusammenfassung:Two recent crystal structures show channel-forming bacterial toxins as soluble monomers (colicin la) or transmembrane pores (α-haemolysin). Together with other data, these structures imply that toxin activity requires dramatic conformational changes.
ISSN:1072-8368
2331-365X
1545-9985
DOI:10.1038/nsb0297-89