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Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation
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2014 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 5, 3254- p.Article in journal (Refereed) Published
Abstract [en]

The mechanisms controlling the conversion of spider silk proteins into insoluble fibres, which happens in a fraction of a second and in a defined region of the silk glands, are still unresolved. The N-terminal domain changes conformation and forms a homodimer when pH is lowered from 7 to 6; however, the molecular details still remain to be determined. Here we investigate site-directed mutants of the N-terminal domain from Euprosthenops australis major ampullate spidroin 1 and find that the charged residues D40, R60 and K65 mediate intersubunit electrostatic interactions. Protonation of E79 and E119 is required for structural conversions of the subunits into a dimer conformation, and subsequent protonation of E84 around pH 5.7 leads to the formation of a fully stable dimer. These residues are highly conserved, indicating that the now proposed three-step mechanism prevents premature aggregation of spidroins and enables fast formation of spider silk fibres in general.

Place, publisher, year, edition, pages
2014. Vol. 5, 3254- p.
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Natural Sciences
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URN: urn:nbn:se:uu:diva-223575DOI: 10.1038/ncomms4254ISI: 000332667600001OAI: oai:DiVA.org:uu-223575DiVA: diva2:713981
Available from: 2014-04-24 Created: 2014-04-22 Last updated: 2017-12-05Bibliographically approved

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Knight, Stefan D.

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