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データを開く
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基本情報
登録情報 | データベース: SASBDB / ID: SASDA37 |
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![]() | Surface Protein G (SasG) EG5 repeat protein G51-G52
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機能・相同性 | ![]() |
生物種 | ![]() ![]() |
![]() | ![]() タイトル: Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. 著者: 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 ...著者: 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 / ![]() ![]() 要旨: 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. |
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構造の表示
構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
-モデル
モデル #235 | ![]() タイプ: atomic / ソフトウェア: SASREF / ダミー原子の半径: 1.90 A / カイ2乗値: 1.1236 ![]() |
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モデル #236 | ![]() タイプ: dummy / ソフトウェア: Gasbor / ダミー原子の半径: 1.90 A / カイ2乗値: 1.1236 ![]() |
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試料
![]() | 名称: Surface Protein G (SasG) EG5 repeat protein G51-G52 / 試料濃度: 7.5 mg/ml |
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バッファ | 名称: Tris / 濃度: 20.00 mM / pH: 7.5 / 組成: 200 mM NaCl, 1 mM EDTA, 20 mM Tris.Cl |
要素 #140 | 名称: SasG / タイプ: protein / 記述: Surface protein G / 分子量: 23.729 / 分子数: 1 / 由来: Staphylococcus aureus / 参照: UniProt: Q2G2B2 配列: GPHMAPKTIT ELEKKVEEIP FKKERKFNPD LAPGTEKVTR EGQKGEKTIT TPTLKNPLTG VIISKGEPKE EITKDPINEL TEYGPETIAP GHRDEFDPKL PTGEKEEVPG KPGIKNPETG DVVRPPVDSV TKYGPVKGDS IVEKEEIPFE KERKFNPDLA PGTEKVTREG ...配列: GPHMAPKTIT ELEKKVEEIP FKKERKFNPD LAPGTEKVTR EGQKGEKTIT TPTLKNPLTG VIISKGEPKE EITKDPINEL TEYGPETIAP GHRDEFDPKL PTGEKEEVPG KPGIKNPETG DVVRPPVDSV TKYGPVKGDS IVEKEEIPFE KERKFNPDLA PGTEKVTREG QKGEKTITTP TLKNPLTGEI ISKGESKEEI TKDPINELTE YGPET |
-実験情報
ビーム | 設備名称: PETRA III P12 / 地域: Hamburg / 国: Germany ![]() | |||||||||||||||||||||
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検出器 | 名称: Pilatus 2M | |||||||||||||||||||||
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距離分布関数 P(R) |
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結果 | コメント: SAXS was used to determine whether the EG5 repeat forms an extended rod-like structure in solution.
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