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TitleCooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.
Journal, issue, pagesNat Commun, Vol. 6, Page 7271, Year 2015
Publish dateJun 1, 2015
AuthorsDominika T 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 R Potts / Jane Clarke /
PubMed AbstractBacteria 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 ...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.
External linksNat Commun / PubMed:26027519 / PubMed Central
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution1.6 Å
Structure data

SASDA37:
Surface Protein G (SasG) EG5 repeat protein G51-G52
Method: SAXS/SANS

SASDA47:
Surface Protein G (SasG) EG5 repeat protein G51-G53
Method: SAXS/SANS

SASDA57:
Surface Protein G (SasG) EG5 repeat protein G51-G54
Method: SAXS/SANS

SASDA67:
Surface Protein G (SasG) EG5 repeat protein G51-G55
Method: SAXS/SANS

SASDA77:
Surface Protein G (SasG) EG5 repeat protein G51-G56
Method: SAXS/SANS

SASDA87:
Surface Protein G (SasG) EG5 repeat protein G51-G57
Method: SAXS/SANS

PDB-4wve:
Crystal structure of the Staphylococcus aureus SasG G52-E2-G53 module
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • staphylococcus aureus (bacteria)
KeywordsSTRUCTURAL PROTEIN / single-layer beta sheet / biofilm formation / surface

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