SASDB84: CyaA Block V (Adenylate cyclase toxin Block V)

基本情報

• 登録情報: データベース: SASBDB / ID: SASDB84

試料

CyaA Block V

• Adenylate cyclase toxin Block V (protein), CyaA Block V, Bordetella pertussis

機能・相同性

分子機能:

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

ドメイン・相同性:

RTX, pore-forming domain / N-terminal domain in RTX protein / RTX toxin determinant A / Haemolysin-type calcium binding-related / Haemolysin-type calcium binding protein related domain / : / Anthrax toxin, edema factor, central / Anthrax toxin, edema factor, C-terminal / Anthrax toxin, edema factor, central domain superfamily / Anthrax toxin LF subunit / Hemolysin-type calcium-binding conserved site / Hemolysin-type calcium-binding region signature. / RTX calcium-binding nonapeptide repeat / RTX calcium-binding nonapeptide repeat (4 copies) / Serralysin-like metalloprotease, C-terminal

構成要素:

Bifunctional hemolysin/adenylate cyclase

• 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, 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.

登録者

• Michael Kachala (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

モデル

• モデル #485: ; タイプ: dummy / ソフトウェア: DAMMIF / ダミー原子の半径: 1.75 A / カイ2乗値: 2.128681; Omokage検索でこの集合体の類似形状データを探す (詳細)

試料

• 試料: 名称: CyaA Block V / 試料濃度: 1.30-5.00
• 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 #317

名称: CyaA Block V / タイプ: protein / 記述: Adenylate cyclase toxin Block V / 分子量: 16 / 分子数: 1 / 由来: Bordetella pertussis / 参照: UniProt: P0DKX7
配列:

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
• 検出器: 名称: Pilatus 2M

スキャン

タイトル: CyaA Block 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 /

	Min	Max
Q	0.0817	3.1872

距離分布関数 P(R)

ソフトウェア P(R): GNOM 4.5a / ポイント数: 389 /

	Min	Max
Q	0.1186	3.185
P(R) point	14	402
R	0	5.541

結果

D max: 5.9 / カーブのタイプ: merged / Standard: BSA

	実験値	Standard	Porod
分子量	13 kDa	13 kDa	14 kDa
体積	-	-	24 nm3

	P(R)	Guinier
前方散乱 I0	2430	2266.34
慣性半径, Rg	1.8 nm	1.8 nm