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- EMDB-3222: Structure of a Chaperone-Usher pilus reveals the molecular basis ... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-3222 | |||||||||
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Title | Structure of a Chaperone-Usher pilus reveals the molecular basis of rod uncoilin | |||||||||
![]() | Reconstruction of P pilus | |||||||||
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![]() | helical polymer / strand donation | |||||||||
Function / homology | Fimbrial-type adhesion domain / Fimbrial protein / Fimbrial-type adhesion domain superfamily / cell adhesion involved in single-species biofilm formation / Adhesion domain superfamily / pilus / extracellular region / Pap fimbrial major pilin protein![]() | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.8 Å | |||||||||
![]() | Hospenthal MK / Redzej A / Dodson K / Ukleja M / Frenz B / Hultgren SJ / DiMaio F / Egelman EH / Waksman G | |||||||||
![]() | ![]() Title: Structure of a Chaperone-Usher Pilus Reveals the Molecular Basis of Rod Uncoiling. Authors: Manuela K Hospenthal / Adam Redzej / Karen Dodson / Marta Ukleja / Brandon Frenz / Catarina Rodrigues / Scott J Hultgren / Frank DiMaio / Edward H Egelman / Gabriel Waksman / ![]() ![]() Abstract: Types 1 and P pili are prototypical bacterial cell-surface appendages playing essential roles in mediating adhesion of bacteria to the urinary tract. These pili, assembled by the chaperone-usher ...Types 1 and P pili are prototypical bacterial cell-surface appendages playing essential roles in mediating adhesion of bacteria to the urinary tract. These pili, assembled by the chaperone-usher pathway, are polymers of pilus subunits assembling into two parts: a thin, short tip fibrillum at the top, mounted on a long pilus rod. The rod adopts a helical quaternary structure and is thought to play essential roles: its formation may drive pilus extrusion by preventing backsliding of the nascent growing pilus within the secretion pore; the rod also has striking spring-like properties, being able to uncoil and recoil depending on the intensity of shear forces generated by urine flow. Here, we present an atomic model of the P pilus generated from a 3.8 Å resolution cryo-electron microscopy reconstruction. This structure provides the molecular basis for the rod's remarkable mechanical properties and illuminates its role in pilus secretion. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 3.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 8.5 KB 8.5 KB | Display Display | ![]() |
Images | ![]() | 113.9 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 310.1 KB | Display | ![]() |
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Full document | ![]() | 309.2 KB | Display | |
Data in XML | ![]() | 5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5fluMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Reconstruction of P pilus | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : P pilus
Entire | Name: P pilus |
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Components |
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-Supramolecule #1000: P pilus
Supramolecule | Name: P pilus / type: sample / ID: 1000 / Number unique components: 1 |
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-Macromolecule #1: PapA
Macromolecule | Name: PapA / type: protein_or_peptide / ID: 1 / Oligomeric state: helical polymer / Recombinant expression: Yes |
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Source (natural) | Organism: ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Date | Jul 8, 2015 |
Image recording | Category: CCD / Film or detector model: FEI FALCON II (4k x 4k) / Number real images: 90 / Average electron dose: 17 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Details | IHRSR |
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Final reconstruction | Applied symmetry - Helical parameters - Δz: 7.7 Å Applied symmetry - Helical parameters - Δ&Phi: 109.8 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 3.8 Å / Resolution method: OTHER / Software - Name: Spider |
CTF correction | Details: Each image |