Gruszka, DT, Whelan, F, Farrance, OE et al. (9 more authors) (2015) Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nature Communications, 6. 7271. 7271 - ?.
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © Author(s) 2015. Creative Commons Attribution 4.0 International License. |
Keywords: | Biological sciences; biophysics; chemical biology |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 28 Jul 2015 12:10 |
Last Modified: | 08 Feb 2018 22:39 |
Published Version: | http://dx.doi.org/10.1038/ncomms8271 |
Status: | Published |
Publisher: | Nature publishing Group |
Identification Number: | 10.1038/ncomms8271 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:88369 |