4wve | pdb_00004wve
Crystal structure of the Staphylococcus aureus SasG G52-E2-G53 module
Structural highlights
FunctionSASG_STAA8 Promotes adhesion of bacterial cells to human squamous nasal epithelial cells, a phenomenon which is likely to be important in nasal colonization. Forms short, extremely dense and thin fibrils all over the bacterial surface. Does not bind to either buccal cells or non-differentiated keratinocytes. Promotes cellular aggregation leading to biofilm formation.[1] [2] Publication Abstract from PubMedBacteria 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. Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.,Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J Nat Commun. 2015 Jun 1;6:7271. doi: 10.1038/ncomms8271. PMID:26027519[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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