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Open data
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Basic information
Entry | Database: PDB / ID: 5ler | ||||||||||||
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Title | Structure of the bacterial sex F pilus (13.2 Angstrom rise) | ||||||||||||
![]() | Pilin | ||||||||||||
![]() | PROTEIN FIBRIL / F-pilus Conjugation Type IV secretion system Phospholipid / Cell adhesion | ||||||||||||
Function / homology | TraA / TraA / extracellular region / plasma membrane / Chem-6V6 / Pilin / Pilin![]() | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 5 Å | ||||||||||||
![]() | Costa, T.R.D. / Ilangovan, I. / Ukleja, M. / Redzej, A. / Santini, J.M. / Smith, T.K. / Egelman, E.H. / Waksman, G. | ||||||||||||
Funding support | ![]() ![]()
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![]() | ![]() Title: Structure of the Bacterial Sex F Pilus Reveals an Assembly of a Stoichiometric Protein-Phospholipid Complex. Authors: Tiago R D Costa / Aravindan Ilangovan / Marta Ukleja / Adam Redzej / Joanne M Santini / Terry K Smith / Edward H Egelman / Gabriel Waksman / ![]() ![]() Abstract: Conjugative pili are widespread bacterial appendages that play important roles in horizontal gene transfer, in spread of antibiotic resistance genes, and as sites of phage attachment. Among ...Conjugative pili are widespread bacterial appendages that play important roles in horizontal gene transfer, in spread of antibiotic resistance genes, and as sites of phage attachment. Among conjugative pili, the F "sex" pilus encoded by the F plasmid is the best functionally characterized, and it is also historically the most important, as the discovery of F-plasmid-mediated conjugation ushered in the era of molecular biology and genetics. Yet, its structure is unknown. Here, we present atomic models of two F family pili, the F and pED208 pili, generated from cryoelectron microscopy reconstructions at 5.0 and 3.6 Å resolution, respectively. These structures reveal that conjugative pili are assemblies of stoichiometric protein-phospholipid units. We further demonstrate that each pilus type binds preferentially to particular phospholipids. These structures provide the molecular basis for F pilus assembly and also shed light on the remarkable properties of conjugative pili in bacterial secretion and phage infection. | ||||||||||||
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 783 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4044MC ![]() 4042C ![]() 4046C ![]() 5legC ![]() 5lfbC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 6831.216 Da / Num. of mol.: 75 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Chemical | ChemComp-6V6 / [( |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: HELICAL ARRAY / 3D reconstruction method: helical reconstruction |
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Sample preparation
Component | Name: F-pilus filament made by an assembly of a stoichiometric protein-phospholipid complex Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: #1 / Source: NATURAL |
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Molecular weight | Value: 7.3 kDa/nm / Experimental value: NO |
Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: Lacey |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Tecnai Polara / Image courtesy: FEI Company |
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Microscopy | Model: FEI POLARA 300 |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 1.67 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
Helical symmerty | Angular rotation/subunit: 27.9 ° / Axial rise/subunit: 13.2 Å / Axial symmetry: C5 | ||||||||||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 5 Å / Resolution method: OTHER / Num. of particles: 11969 / Symmetry type: HELICAL | ||||||||||||||||||||||||||||||||||||||||
Atomic model building | Protocol: AB INITIO MODEL |