+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDA57 |
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Sample | Surface Protein G (SasG) EG5 repeat protein G51-G54
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Function / homology | Function and homology information |
Biological species | Staphylococcus aureus (bacteria) |
Citation | Journal: Nat Commun / Year: 2015 Title: Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Authors: Dominika 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 / ...Authors: Dominika 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 / 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 ...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. |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Models
Model #239 | Type: dummy / Software: Gasbor / Radius of dummy atoms: 1.90 A / Chi-square value: 0.9216 Search similar-shape structures of this assembly by Omokage search (details) |
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Model #240 | Type: atomic / Software: SASREF / Radius of dummy atoms: 1.90 A / Chi-square value: 0.9409 Search similar-shape structures of this assembly by Omokage search (details) |
-Sample
Sample | Name: Surface Protein G (SasG) EG5 repeat protein G51-G54 / Specimen concentration: 6 mg/ml |
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Buffer | Name: Tris / Concentration: 20.00 mM / pH: 7.5 / Composition: 200 mM NaCl, 1 mM EDTA, 20 mM Tris.Cl |
Entity #142 | Name: SasG / Type: protein / Description: Surface protein G / Formula weight: 52.802 / Num. of mol.: 1 / Source: Staphylococcus aureus / References: UniProt: Q2G2B2 Sequence: GPAMAPKTIT ELEKKVEEIP FKKERKFNPD LAPGTEKVTR EGQKGEKTIT TPTLKNPLTG VIISKGEPKE EITKDPINEL TEYGPETIAP GHRDEFDPKL PTGEKEEVPG KPGIKNPETG DVVRPPVDSV TKYGPVKGDS IVEKEEIPFE KERKFNPDLA PGTEKVTREG ...Sequence: GPAMAPKTIT ELEKKVEEIP FKKERKFNPD LAPGTEKVTR EGQKGEKTIT TPTLKNPLTG VIISKGEPKE EITKDPINEL TEYGPETIAP GHRDEFDPKL PTGEKEEVPG KPGIKNPETG DVVRPPVDSV TKYGPVKGDS IVEKEEIPFE KERKFNPDLA PGTEKVTREG QKGEKTITTP TLKNPLTGEI ISKGESKEEI TKDPINELTE YGPETITPGH RDEFDPKLPT GEKEEVPGKP GIKNPETGDV VRPPVDSVTK YGPVKGDSIV EKEEIPFEKE RKFNPDLAPG TEKVTREGQK GEKTITTPTL KNPLTGVIIS KGEPKEEITK DPINELTEYG PETITPGHRD EFDPKLPTGE KEEVPGKPGI KNPETGDVVR PPVDSVTKYG PVKGDSIVEK EEIPFKKERK FNPDLAPGTE KVTREGQKGE KTITTPTLKN PLTGEIISKG ESKEEITKDP INELTEYGPE TWSHPQFEK |
-Experimental information
Beam | Instrument name: PETRA III P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron / Wavelength: 0.12 Å / Dist. spec. to detc.: 3.1 mm | |||||||||||||||||||||
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Detector | Name: Pilatus 2M | |||||||||||||||||||||
Scan | Title: G51-G54 / Measurement date: Nov 12, 2013 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
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Distance distribution function P(R) | Sofotware P(R): GNOM 4.6 / Number of points: 405 /
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Result | D max: 38.5 / Type of curve: single_conc Comments: SAXS was used to determine whether the EG5 repeat forms an extended rod-like structure in solution.
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