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PMID:16688219

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Citation

Eifler, N, Vetsch, M, Gregorini, M, Ringler, P, Chami, M, Philippsen, A, Fritz, A, Müller, SA, Glockshuber, R, Engel, A and Grauschopf, U (2006) Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state. EMBO J. 25:2652-61

Abstract

ClyA is a pore-forming toxin from virulent Escherichia coli and Salmonella enterica strains. Here, we show that the intrinsic hemolytic activity of ClyA is independent of its redox state, and that the assembly of both reduced and oxidized ClyA to the ring-shaped oligomer is triggered by contact with lipid or detergent. A rate-limiting conformational transition in membrane-bound ClyA monomers precedes their assembly to the functional pore. We obtained a three-dimensional model of the detergent-induced oligomeric complex at 12 A resolution by combining cryo- and negative stain electron microscopy with mass measurements by scanning transmission electron microscopy. The model reveals that 13 ClyA monomers assemble into a cylinder with a hydrophobic cap region, which may be critical for membrane insertion.

Links

PubMed PMC1478193 Online version:10.1038/sj.emboj.7601130

Keywords

Cysteine/chemistry; Detergents/chemistry; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Escherichia coli Proteins/ultrastructure; Hemolysin Proteins/chemistry; Hemolysin Proteins/metabolism; Hemolysin Proteins/ultrastructure; Lipids/chemistry; Microscopy, Electron; Models, Molecular; Oxidation-Reduction; Protein Structure, Quaternary

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:HLYE

enables

GO:0042802: identical protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P77335

F

Seeded From UniProt

complete

Notes

See also

References

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