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• W2068503513 abstract "The periplasmic Yersinia pestis molecular chaperone Caf1M belongs to a superfamily of bacterial proteins for one of which (PapD protein of Escherichia coli) the immunoglobulin-like fold was solved by X-ray analysis. The N-terminal domain of Caf1M was found to share a 20% amino acid sequence identity with an inclusion body-associated protein IbpB of Escherichia coli. One of the regions that was compared, was 32 amino acids long, and displayed more than 40% identity, probability of random coincidence was 1.2 x 10(-4). IbpB is involved in a superfamily of small heat shock proteins which fulfil the function of molecular chaperone. On the basis of the revealed homology, an immunoglobulin-like one-domain model of IbpB three-dimensional structure was designed which could be a prototype conformation of sHsp's. The structure suggested is in good agreement with the known experimental data obtained for different members of sHsp's superfamily." @default.
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• W2068503513 date "1995-07-01" @default.
• W2068503513 modified "2023-09-25" @default.
• W2068503513 title "Structural and functional homology between periplasmic bacterial molecular chaperones and small heat shock proteins" @default.
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• W2068503513 doi "https://doi.org/10.1111/j.1574-695x.1995.tb00155.x" @default.
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