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Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface
Lund Univ, MAX IV Lab, POB 118, SE-22100 Lund, Sweden..
Lund Univ, Ctr Mol Prot Sci, Dept Biochem & Struct Biol, POB 124, SE-22100 Lund, Sweden..
Lund Univ, Ctr Mol Prot Sci, Dept Biochem & Struct Biol, POB 124, SE-22100 Lund, Sweden..
Lund Univ, Ctr Mol Prot Sci, Dept Biochem & Struct Biol, POB 124, SE-22100 Lund, Sweden..
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2018 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 8, article id 5199Article in journal (Refereed) Published
Abstract [en]

= The remarkably efficient suppression of amyloid fibril formation by the DNAJB6 chaperone is dependent on a set of conserved S/T-residues and an oligomeric structure, features unusual among DNAJ chaperones. We explored the structure of DNAJB6 using a combination of structural methods. Lysine-specific crosslinking mass spectrometry provided distance constraints to select a homology model of the DNAJB6 monomer, which was subsequently used in crosslink-assisted docking to generate a dimer model. A peptide-binding cleft lined with S/T-residues is formed at the monomer-monomer interface. Mixed isotope crosslinking showed that the oligomers are dynamic entities that exchange subunits. The purified protein is well folded, soluble and composed of oligomers with a varying number of subunits according to small-angle X-ray scattering (SAXS). Elongated particles (160 x 120 angstrom) were detected by electron microscopy and single particle reconstruction resulted in a density map of 20 angstrom resolution into which the DNAJB6 dimers fit. The structure of the oligomer and the S/T-rich region is of great importance for the understanding of the function of DNAJB6 and how it can bind aggregation-prone peptides and prevent amyloid diseases.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP , 2018. Vol. 8, article id 5199
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Biological Sciences
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URN: urn:nbn:se:kth:diva-225706DOI: 10.1038/s41598-018-23035-9ISI: 000428235200003PubMedID: 29581438Scopus ID: 2-s2.0-85044502155OAI: oai:DiVA.org:kth-225706DiVA, id: diva2:1196788
Note

QC 20180411

Available from: 2018-04-11 Created: 2018-04-11 Last updated: 2018-04-11Bibliographically approved

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