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Structure of the N-terminal domain of Euprosthenops australis dragline silk suggests that conversion of spidroin dope to spider silk involves a conserved asymmetric dimer intermediate
Uppsala Univ, Dept Cell & Mol Biol, Biomed Ctr, POB 596, SE-75124 Uppsala, Sweden..
Uppsala Univ, Dept Cell & Mol Biol, Biomed Ctr, POB 596, SE-75124 Uppsala, Sweden..
Vrije Univ Brussel, Struct Biol Brussels, B-1050 Brussels, Belgium.;VIB VUB Ctr Struct Biol, B-1050 Brussels, Belgium..
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Protein Technology.ORCID iD: 0000-0003-0140-419X
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2019 (English)In: Acta Crystallographica Section D: Structural Biology, ISSN 2059-7983, Vol. 75, p. 618-627Article in journal (Refereed) Published
Abstract [en]

Spider silk is a biomaterial with exceptional mechanical toughness, and there is great interest in developing biomimetic methods to produce engineered spider silk-based materials. However, the mechanisms that regulate the conversion of spider silk proteins (spidroins) from highly soluble dope into silk are not completely understood. The N-terminal domain (NT) of Euprosthenops australis dragline silk protein undergoes conformational and quaternary-structure changes from a monomer at a pH above 7 to a homodimer at lower pH values. Conversion from the monomer to the dimer requires the protonation of three conserved glutamic acid residues, resulting in a low-pH 'locked' dimer stabilized by symmetric electrostatic interactions at the poles of the dimer. The detailed molecular events during this transition are still unresolved. Here, a 2.1 angstrom resolution crystal structure of an NT T61A mutant in an alternative, asymmetric, dimer form in which the electrostatic interactions at one of the poles are dramatically different from those in symmetrical dimers is presented. A similar asymmetric dimer structure from dragline silk of Nephila clavipes has previously been described. It is suggested that asymmetric dimers represent a conserved intermediate state in spider silk formation, and a revised 'lock-and-trigger' mechanism for spider silk formation is presented.

Place, publisher, year, edition, pages
International Union of Crystallography , 2019. Vol. 75, p. 618-627
Keywords [en]
spider silk, assembly, pH relay, spidroin, N-terminal domain, Euprosthenops australis
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-255392DOI: 10.1107/S2059798319007253ISI: 000474450300001PubMedID: 31282471Scopus ID: 2-s2.0-85068718706OAI: oai:DiVA.org:kth-255392DiVA, id: diva2:1339506
Note

QC 20190730

Available from: 2019-07-30 Created: 2019-07-30 Last updated: 2019-07-30Bibliographically approved

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