- EMDB-20114: CryoEM structure of PilB from Geobacter metallireducens: C2ccocco... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-20114
タイトル
CryoEM structure of PilB from Geobacter metallireducens: C2ccocco conformation
マップデータ
Sharpened and z-flipped map
試料
複合体: PilB Hexamer
タンパク質・ペプチド: Type IV pilus biogenesis ATPase PilB
キーワード
ATPase / T4P / type iv pilus / motor / MOTOR PROTEIN
機能・相同性
機能・相同性情報
pilus assembly / ATP hydrolysis activity / ATP binding / metal ion binding / plasma membrane / cytoplasm 類似検索 - 分子機能
ATPase, type IV, pilus assembly, PilB / Type II secretion system protein GspE, N-terminal / MshEN domain / Type II secretion system protein GspE, N-terminal superfamily / Bacterial type II secretion system protein E signature. / Type II/IV secretion system protein / Type II/IV secretion system protein / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性
ジャーナル: Nat Commun / 年: 2019 タイトル: Multiple conformations facilitate PilT function in the type IV pilus. 著者: Matthew McCallum / Samir Benlekbir / Sheryl Nguyen / Stephanie Tammam / John L Rubinstein / Lori L Burrows / P Lynne Howell / 要旨: Type IV pilus-like systems are protein complexes that polymerize pilin fibres. They are critical for virulence in many bacterial pathogens. Pilin polymerization and depolymerization are powered by ...Type IV pilus-like systems are protein complexes that polymerize pilin fibres. They are critical for virulence in many bacterial pathogens. Pilin polymerization and depolymerization are powered by motor ATPases of the PilT/VirB11-like family. This family is thought to operate with C symmetry; however, most of these ATPases crystallize with either C or C symmetric conformations. The relevance of these conformations is unclear. Here, we determine the X-ray structures of PilT in four unique conformations and use these structures to classify the conformation of available PilT/VirB11-like family member structures. Single particle electron cryomicroscopy (cryoEM) structures of PilT reveal condition-dependent preferences for C C, and C conformations. The physiologic importance of these conformations is validated by coevolution analysis and functional studies of point mutants, identifying a rare gain-of-function mutation that favours the C conformation. With these data, we propose a comprehensive model of PilT function with broad implications for PilT/VirB11-like family members.