E. coli <FONT FACE=Symbol>a</FONT>-hemolysin: a membrane-active protein toxin

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E . coli α - hemolysin : a membrane - active protein toxin

α-Hemolysin is synthesized as a 1024-amino acid polypeptide, then intracellularly activated by specific fatty acylation. A second activation step takes place in the extracellular medium through binding of Ca2+ ions. Even in the absence of fatty acids and Ca2+ HlyA is an amphipathic protein, with a tendency to self-aggregation. However, Ca2+-binding appears to expose hydrophobic patches on the p...

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Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function.

The pore-forming hemolysin (HlyA) of Escherichia coli represents a unique class of bacterial toxins that require a posttranslational modification for activity. The inactive protoxin pro-HlyA is activated intracellularly by amide linkage of fatty acids to two internal lysine residues 126 amino acids apart, directed by the cosynthesized HlyC protein with acyl carrier protein as the fatty acid don...

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The ultimate aim of biochemistry is to decipher how events occur inside of living cells or organisms. The living cell must also be regarded as the ideal model system for any biochemical application, as most physiological targets are found inside living cells. The cell envelope of the Gram-negative bacterium Escherichia coli is a complex structure and many of the proteins found in the bacterial ...

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Cloning and expression of Brucella outer membrane protein 36kDa (OMP2b) in E. coli

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E. coli Hemolysin E (HlyE, ClyA, SheA) X-Ray Crystal Structure of the Toxin and Observation of Membrane Pores by Electron Microscopy

Hemolysin E (HlyE) is a novel pore-forming toxin of Escherichia coli, Salmonella typhi, and Shigella flexneri. Here we report the X-ray crystal structure of the water-soluble form of E. coli HlyE at 2.0 A resolution and the visualization of the lipid-associated form of the toxin in projection at low resolution by electron microscopy. The crystal structure reveals HlyE to be the first member of ...

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ژورنال

عنوان ژورنال: Brazilian Journal of Medical and Biological Research

سال: 1998

ISSN: 0100-879X

DOI: 10.1590/s0100-879x1998000800002