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-Structure paper
タイトル | Multiple conformations facilitate PilT function in the type IV pilus. |
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ジャーナル・号・ページ | Nat Commun, Vol. 10, Issue 1, Page 5198, Year 2019 |
掲載日 | 2019年11月15日 |
著者 | Matthew McCallum / Samir Benlekbir / Sheryl Nguyen / Stephanie Tammam / John L Rubinstein / Lori L Burrows / P Lynne Howell / |
PubMed 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. |
リンク | Nat Commun / PubMed:31729381 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 1.892 - 7.8 Å |
構造データ | EMDB-20114, PDB-6olj: EMDB-20115, PDB-6olk: EMDB-20116, PDB-6oll: EMDB-20117, PDB-6olm: PDB-6ojx: PDB-6ojy: PDB-6ojz: PDB-6ok2: PDB-6okv: |
化合物 | ChemComp-EDO: ChemComp-MG: ChemComp-ATP: ChemComp-HOH: ChemComp-SO4: ChemComp-ADP: ChemComp-ANP: |
由来 |
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キーワード | MOTOR PROTEIN / T4P / ATPase / type IV pilus / motor |