+データを開く
-基本情報
登録情報 | データベース: SASBDB / ID: SASDB74 |
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試料 | CyaA Block I-V
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機能・相同性 | 機能・相同性情報 calcium- and calmodulin-responsive adenylate cyclase activity / hemolysis in another organism / adenylate cyclase / cAMP biosynthetic process / adenylate cyclase activity / channel activity / toxin activity / positive regulation of cytosolic calcium ion concentration / calmodulin binding / calcium ion binding ...calcium- and calmodulin-responsive adenylate cyclase activity / hemolysis in another organism / adenylate cyclase / cAMP biosynthetic process / adenylate cyclase activity / channel activity / toxin activity / positive regulation of cytosolic calcium ion concentration / calmodulin binding / calcium ion binding / host cell plasma membrane / extracellular region / ATP binding / membrane 類似検索 - 分子機能 |
生物種 | Bordetella pertussis (百日咳菌) |
引用 | ジャーナル: Mol Cell / 年: 2016 タイトル: Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. 著者: Ladislav Bumba / Jiri Masin / Pavel Macek / Tomas Wald / Lucia Motlova / Ilona Bibova / Nela Klimova / Lucie Bednarova / Vaclav Veverka / Michael Kachala / Dmitri I Svergun / Cyril Barinka / Peter Sebo / 要旨: Calcium-binding RTX proteins are equipped with C-terminal secretion signals and translocate from the Ca(2+)-depleted cytosol of Gram-negative bacteria directly into the Ca(2+)-rich external milieu, ...Calcium-binding RTX proteins are equipped with C-terminal secretion signals and translocate from the Ca(2+)-depleted cytosol of Gram-negative bacteria directly into the Ca(2+)-rich external milieu, passing through the "channel-tunnel" ducts of type I secretion systems (T1SSs). Using Bordetella pertussis adenylate cyclase toxin, we solved the structure of an essential C-terminal assembly that caps the RTX domains of RTX family leukotoxins. This is shown to scaffold directional Ca(2+)-dependent folding of the carboxy-proximal RTX repeat blocks into β-rolls. The resulting intramolecular Brownian ratchets then prevent backsliding of translocating RTX proteins in the T1SS conduits and thereby accelerate excretion of very large RTX leukotoxins from bacterial cells by a vectorial "push-ratchet" mechanism. Successive Ca(2+)-dependent and cosecretional acquisition of a functional RTX toxin structure in the course of T1SS-mediated translocation, through RTX domain folding from the C-terminal cap toward the N terminus, sets a paradigm that opens for design of virulence inhibitors of major pathogens. |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-モデル
モデル #484 | タイプ: dummy / ソフトウェア: DAMMIF / ダミー原子の半径: 4.75 A / カイ2乗値: 0.839056 Omokage検索でこの集合体の類似形状データを探す (詳細) |
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-試料
試料 | 名称: CyaA Block I-V / 試料濃度: 1.10-4.40 |
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バッファ | 名称: Tris HCl / 濃度: 10.00 mM / pH: 8 / 組成: 150 mM NaCl, 10 mM CaCl2 |
要素 #316 | 名称: CyaA Block I-V / タイプ: protein / 記述: Adenylate cyclase toxin Block I-V / 分子量: 70 / 分子数: 1 / 由来: Bordetella pertussis / 参照: UniProt: P0DKX7 配列: EGDIHMSPIL GYWKIKGLVQ PTRLLLEYLE EKYEEHLYER DEGDKWRNKK FELGLEFPNL PYYIDGDVKL TQSMAIIRYI ADKHNMLGGC PKERAEISML EGAVLDIRYG VSRIAYSKDF ETLKVDFLSK LPEMLKMFED RLCHKTYLNG DHVTHPDFML YDALDVVLYM ...配列: EGDIHMSPIL GYWKIKGLVQ PTRLLLEYLE EKYEEHLYER DEGDKWRNKK FELGLEFPNL PYYIDGDVKL TQSMAIIRYI ADKHNMLGGC PKERAEISML EGAVLDIRYG VSRIAYSKDF ETLKVDFLSK LPEMLKMFED RLCHKTYLNG DHVTHPDFML YDALDVVLYM DPMCLDAFPK LVCFKKRIEA IPQIDKYLKS SKYIAWPLQG WQATFGGGDH PPKSDGSTSG SGHHHHHHSA GLVPRGSTAI GMKETAAAKF ERQHMDSPDL GTGGGSGIEG Renlyfqgle hvqhiiggag ndsitgnahd nflaggsgdd rldggagndt lvggegqntv iggagddvfl qdlgvwsnql dggagvdtvk ynvhqpseer lermgdtgih adlqkgtvek wpalnlfsvd hvknienlhg srlndriagd dqdnelwghd gndtirgrgg ddilrgglgl dtlygedgnd iflqddetvs ddidggagld tvdysamihp grivapheyg fgieadlsre wvrkasalgv dyydnvrnve nvigtsmkdv ligdaqantl mgqggddtvr ggdgddllfg gdgndmlygd agndtlyggl gddtleggag ndwfgqtqar ehdvlrggdg vdtvdysqtg ahagiaagri glgiladlga grvdklgeag ssaydtvsgi envvgtelad ritgdaqanv lrgaggadvl aggegddvll ggdgddqlsg dagrdrlyge agddwffqda anagnlldgg dgrdtvdfsg pgrgldagak gvflslgkgf aslmdepets nvlrnienav gsarddvlig daganvlngl agndvlsgga gddvllgdeg sdllsgdagn ddlfggqgdd tylfgvgygh dtiyesgggh dtirinagad qlwfarqgnd leirilgtdd altvhdwyrd adhrveiiha anqavdqagi eklveamaqy pdp |
-実験情報
ビーム | 設備名称: PETRA III P12 / 地域: Hamburg / 国: Germany / 線源: X-ray synchrotron / 波長: 0.12 Å / スペクトロメータ・検出器間距離: 3.1 mm | |||||||||||||||||||||
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検出器 | 名称: Pilatus 2M | |||||||||||||||||||||
スキャン | タイトル: CyaA Block I-V / 測定日: 2013年10月31日 / 保管温度: 10 °C / セル温度: 10 °C / 照射時間: 0.05 sec. / フレーム数: 20 / 単位: 1/nm /
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距離分布関数 P(R) | ソフトウェア P(R): GNOM 4.6 / ポイント数: 503 /
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結果 | D max: 17.15 / カーブのタイプ: extrapolated / Standard: BSA
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