Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Multiple conformations facilitate PilT function in the type IV pilus.
Journal, issue, pages	Nat Commun, Vol. 10, Issue 1, Page 5198, Year 2019
Publish date	Nov 15, 2019
Authors	Matthew McCallum / Samir Benlekbir / Sheryl Nguyen / Stephanie Tammam / John L Rubinstein / Lori L Burrows / P Lynne Howell /
PubMed Abstract	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.
External links	Nat Commun / PubMed:31729381 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.892 - 7.8 Å
Structure data	20114 6olj EMDB-20114, PDB-6olj: CryoEM structure of PilB from Geobacter metallireducens: C2ccocco conformation Method: EM (single particle) / Resolution: 7.8 Å 20115 6olk EMDB-20115, PDB-6olk: CryoEM structure of PilT4 from Geobacter metallireducens without adding nucleotide: C3ocococ conformation Method: EM (single particle) / Resolution: 4.0 Å 20116 6oll EMDB-20116, PDB-6oll: CryoEM structure of PilT4 from Geobacter metallireducens without adding nucleotide: C2oocooc conformation Method: EM (single particle) / Resolution: 4.1 Å 20117 6olm EMDB-20117, PDB-6olm: CryoEM structure of PilT4 from Geobacter metallireducens with added ATP: C6cccccc conformation Method: EM (single particle) / Resolution: 4.4 Å PDB-6ojx: PilT4 from Geobacter metallireducens bound to ATP Method: X-RAY DIFFRACTION / Resolution: 1.892 Å PDB-6ojy: Methylated PilT4 from Geobacter metallireducens bound to sulfate: C3ocococ conformation Method: X-RAY DIFFRACTION / Resolution: 3.3 Å PDB-6ojz: PilT4 from Geobacter metallireducens bound to ADP with partial occupancy: C3ocococ conformation Method: X-RAY DIFFRACTION / Resolution: 3.027 Å PDB-6ok2: PilT4 from Geobacter metallireducens bound to ADP: C3ocococ conformation Method: X-RAY DIFFRACTION / Resolution: 3.287 Å PDB-6okv: PilT4 from Geobacter metallireducens bound to AMP-PNP: C2ccocco conformation Method: X-RAY DIFFRACTION / Resolution: 4.007 Å
Chemicals	ChemComp-EDO: 1,2-ETHANEDIOL ChemComp-MG: Unknown entry ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-HOH: WATER ChemComp-SO4: SULFATE ION ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM
Source	Geobacter metallireducens (bacteria) geobacter metallireducens (strain gs-15 / atcc 53774 / dsm 7210) (bacteria)
Keywords	MOTOR PROTEIN / T4P / ATPase / type IV pilus / motor