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Instruments / Technical Area	Publication Details	Published	Actions
I04-Macromolecular Crystallography	Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein Dominika Gruszka , Fiona Whelan , Oliver E. Farrance , Herman K. H. Fung , Emanuele Paci , Cy M. Jeffries , Dmitri I. Svergun , Clair Baldock , Christoph G. Baumann , David J. Brockwell , Jennifer Potts , Jane Clarke Nature Communications 6, 1015-1030 DOI: 10.1038/ncomms8271 PMID: 26027519 Diamond Proposal Number(s): [7864] Open Access Show Abstract ▼ 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.	Jun 2015

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I04-Macromolecular Crystallography

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