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Identification of residues for chaperone-like activity of OppA protein in Yersinia pseudotuberculosis
Elena Escobar Garduño1, Thomas Scior2, Lucia Soto Urzúa1
1Centro de Investigaciones en Ciencias Microbiológicas, Instituto de Ciencias, IC-11 CU San Manuel, Benemérita Universidad Autónoma de Puebla, Puebla, México.
Abstract:
Periplasmic oligopeptide binding protein (OppA) is part of a multimeric cytoplasmic membrane protein complex, whose function is known as peptide transporters found in Gram-negative bacteria. A chaperone-like activity has been found for the OppA from Yersinia pseudotuberculosis, using biochemical experiments. Through computational analysis, we selected two amino acid residues (R41 and D42) that probably are involved in the chaperone-like activity. Our results to corroborate how OppA assists refolding and renaturation of lactate dehydrogenase and alpha-glucosidase denatured enzymes.
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