Self-assembly of spider silk proteins is controlled by a pH-sensitive relay

Glareh Askarieh, My Hedhammar, Kerstin Nordling, Alejandra Saenz, Cristina Casals, Anna Rising, Jan Johansson () and Stefan D. Knight ()
Additional contact information
Glareh Askarieh: Oslo University, 1033 Blindern, 0315 Oslo, Norway
My Hedhammar: Physiology and Biochemistry, SLU, Biomedical Centre, P.O. Box 575, SE-751 23 Uppsala, Sweden
Kerstin Nordling: Physiology and Biochemistry, SLU, Biomedical Centre, P.O. Box 575, SE-751 23 Uppsala, Sweden
Alejandra Saenz: Complutense University of Madrid
Cristina Casals: Complutense University of Madrid
Anna Rising: Physiology and Biochemistry, SLU, Biomedical Centre, P.O. Box 575, SE-751 23 Uppsala, Sweden
Jan Johansson: Physiology and Biochemistry, SLU, Biomedical Centre, P.O. Box 575, SE-751 23 Uppsala, Sweden
Stefan D. Knight: Uppsala BioCenter, SLU, Biomedical Centre, P.O. Box 590, SE-751 24 Uppsala, Sweden

Nature, 2010, vol. 465, issue 7295, 236-238

Abstract: Spider silk's dual identity Many proteins form fibrillar structures at high concentrations, but spider silk proteins, with highly repetitive segments flanked by non-repetitive (NR) terminal domains, behave differently. They are remarkably soluble when stored at high concentration yet can convert to extremely sturdy fibres on demand. The molecular mechanism that makes this possible is not yet clear, but two structural studies in this issue provide new clues. Askarieh et al. present the 1.7 Å X-ray crystal structure of the N-terminal domain of a dragline spidroin from the nursery web spider Euprosthenops australis. The structure shows how this highly conserved domain can regulate silk assembly by preventing premature aggregation of spidroins and triggering polymerization as the pH falls along the silk extrusion duct. Hagn et al. determined the solution structure of the C-terminal NR domain of the dragline silk protein fibroin 3 from the common orb-weaver Araneus diadematus. They observe a conformational switch, activated by chemical or mechanical stimuli, between storage and assembly forms of the protein.

Date: 2010
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DOI: 10.1038/nature08962

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