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Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein

DOI: 10.1038/ncomms8271 DOI Help
PMID: 26027519 PMID Help

Authors: Dominika Gruszka (University of York) , Fiona Whelan (University of York) , Oliver E. Farrance (University of Leeds) , Herman K. H. Fung (University of York) , Emanuele Paci (University of Leeds) , Cy M. Jeffries (European Molecular Biology Laboratory) , Dmitri I. Svergun (European Molecular Biology Laboratory) , Clair Baldock (University of Manchester) , Christoph G. Baumann (University of York) , David J. Brockwell (University of Leeds) , Jennifer Potts (University of York) , Jane Clarke (University of Cambridge)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 6 , PAGES 1015-1030

State: Published (Approved)
Published: June 2015
Diamond Proposal Number(s): 7864

Open Access Open Access

Abstract: Bacteria exploit surface proteins to adhere to other bacteria, surfaces and host cells. Such proteins need to project away from the bacterial surface and resist significant mechanical forces. SasG is a protein that forms extended fibrils on the surface of Staphylococcus aureus and promotes host adherence and biofilm formation. Here we show that although monomeric and lacking covalent cross-links, SasG maintains a highly extended conformation in solution. This extension is mediated through obligate folding cooperativity of the intrinsically disordered E domains that couple non-adjacent G5 domains thermodynamically, forming interfaces that are more stable than the domains themselves. Thus, counterintuitively, the elongation of the protein appears to be dependent on the inherent instability of its domains. The remarkable mechanical strength of SasG arises from tandemly arrayed ‘clamp’ motifs within the folded domains. Our findings reveal an elegant minimal solution for the assembly of monomeric mechano-resistant tethers of variable length.

Journal Keywords: Biological Sciences; Biophysics; Chemical Biology

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

Added On: 29/09/2015 10:10

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