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• W3027901181 endingPage "106406" @default.
• W3027901181 startingPage "106406" @default.
• W3027901181 abstract "HdeA is a small acid-stress chaperone protein found in the periplasm of several pathogenic gram-negative bacteria. In neutral pH environments HdeA is an inactive folded homodimer but when exposed to strong acidic environments it partially unfolds and, once activated, binds to other periplasmic proteins, protecting them from irreversible aggregation. Here we use a combination of hydrogen/deuterium exchange NMR experiments and constant pH molecular dynamics simulations to elucidate the role of HdeA’s N-terminus in its activation mechanism. Previous work indicates that the N-terminus is flexible and unprotected at high pH while exhibiting interactions with some HdeA client binding site residues. It, however, becomes partially solvent-protected at pH 2.6 – 2.8 and then loses protection again at pH 2.0. This protection is not due to the appearance of new secondary structure, but rather increased contacts between N-terminal residues and the C-terminus of the other protomer in the dimer, as well as concurrent loosening of its hold on the client binding site residues, priming HdeA for interactions with periplasmic client proteins. This work also uncovers unusual protonation profiles of some titratable residues and suggests their complex role in chaperone function." @default.
• W3027901181 created "2020-05-29" @default.
• W3027901181 creator A5001624505 @default.
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• W3027901181 date "2020-09-01" @default.
• W3027901181 modified "2023-10-15" @default.
• W3027901181 title "The complex role of the N-terminus and acidic residues of HdeA as pH-dependent switches in its chaperone function" @default.
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• W3027901181 doi "https://doi.org/10.1016/j.bpc.2020.106406" @default.
• W3027901181 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8276670" @default.
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