5LEG

Structure of the bacterial sex F pilus (pED208)


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.60 Å
  • Aggregation State: HELICAL ARRAY 
  • Reconstruction Method: HELICAL 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structure of the Bacterial Sex F Pilus Reveals an Assembly of a Stoichiometric Protein-Phospholipid Complex.

Costa, T.R.Ilangovan, A.Ukleja, M.Redzej, A.Santini, J.M.Smith, T.K.Egelman, E.H.Waksman, G.

(2016) Cell 166: 1436-1444.e10

  • DOI: https://doi.org/10.1016/j.cell.2016.08.025
  • Primary Citation of Related Structures:  
    5LEG, 5LER, 5LFB

  • PubMed 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, 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.


  • Organizational Affiliation

    Institute of Structural and Molecular Biology, University College London and Birkbeck, Malet Street, London WC1E 7HX, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Pilin63Salmonella enterica subsp. enterica serovar TyphiMutation(s): 0 
UniProt
Find proteins for P12060 (Salmonella typhi)
Explore P12060 
Go to UniProtKB:  P12060
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP12060
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
LHG
Query on LHG

Download Ideal Coordinates CCD File 
AD [auth 2J]
AE [auth 4F]
BD [auth 2K]
BE [auth 4G]
CC [auth 1A]
AD [auth 2J],
AE [auth 4F],
BD [auth 2K],
BE [auth 4G],
CC [auth 1A],
CD [auth 2L],
CE [auth 4H],
DC [auth 1B],
DD [auth 2M],
DE [auth 4I],
EC [auth 1C],
ED [auth 2N],
EE [auth 4J],
FC [auth 1D],
FD [auth 2O],
FE [auth 4K],
GC [auth 1E],
GD [auth 3A],
GE [auth 4L],
HC [auth 1F],
HD [auth 3B],
HE [auth 4M],
IC [auth 1G],
ID [auth 3C],
IE [auth 4N],
JC [auth 1H],
JD [auth 3D],
JE [auth 4O],
KC [auth 1I],
KD [auth 3E],
KE [auth 5A],
LC [auth 1J],
LD [auth 3F],
LE [auth 5B],
MC [auth 1K],
MD [auth 3G],
ME [auth 5C],
NC [auth 1L],
ND [auth 3H],
NE [auth 5D],
OC [auth 1M],
OD [auth 3I],
OE [auth 5E],
PC [auth 1N],
PD [auth 3J],
PE [auth 5F],
QC [auth 1O],
QD [auth 3K],
QE [auth 5G],
RC [auth 2A],
RD [auth 3L],
RE [auth 5H],
SC [auth 2B],
SD [auth 3M],
SE [auth 5I],
TC [auth 2C],
TD [auth 3N],
TE [auth 5J],
UC [auth 2D],
UD [auth 3O],
UE [auth 5K],
VC [auth 2E],
VD [auth 4A],
VE [auth 5L],
WC [auth 2F],
WD [auth 4B],
WE [auth 5M],
XC [auth 2G],
XD [auth 4C],
XE [auth 5N],
YC [auth 2H],
YD [auth 4D],
YE [auth 5O],
ZC [auth 2I],
ZD [auth 4E]
1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
C38 H75 O10 P
BIABMEZBCHDPBV-MPQUPPDSSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.60 Å
  • Aggregation State: HELICAL ARRAY 
  • Reconstruction Method: HELICAL 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONIHRSR,SPIDER22
MODEL REFINEMENTPHENIX1.10.1-2155

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Wellcome TrustUnited Kingdom098302
Wellcome TrustUnited Kingdom093228
National Institutes of HealthUnited StatesGM035269

Revision History  (Full details and data files)

  • Version 1.0: 2016-09-28
    Type: Initial release
  • Version 1.1: 2017-08-02
    Changes: Data collection