5LER

Structure of the bacterial sex F pilus (13.2 Angstrom rise)


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 5.00 Å
  • Aggregation State: HELICAL ARRAY 
  • Reconstruction Method: HELICAL 

wwPDB Validation   3D Report Full Report


This is version 1.3 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
Pilin65Escherichia coliMutation(s): 0 
UniProt
Find proteins for P04737 (Escherichia coli (strain K12))
Explore P04737 
Go to UniProtKB:  P04737
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP04737
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
6V6
Query on 6V6

Download Ideal Coordinates CCD File 
AC [auth 1D]
AD [auth 3B]
AE [auth 4N]
BC [auth 1E]
BD [auth 3C]
AC [auth 1D],
AD [auth 3B],
AE [auth 4N],
BC [auth 1E],
BD [auth 3C],
BE [auth 5A],
CC [auth 1F],
CD [auth 3D],
CE [auth 5B],
DC [auth 1G],
DD [auth 3E],
DE [auth 5C],
EC [auth 1H],
ED [auth 3F],
EE [auth 5D],
FC [auth 1I],
FD [auth 3G],
FE [auth 5E],
GC [auth 1J],
GD [auth 3H],
GE [auth 5F],
HC [auth 1K],
HD [auth 3I],
HE [auth 5G],
IC [auth 1L],
ID [auth 3J],
IE [auth 5H],
JC [auth 1M],
JD [auth 3K],
JE [auth 5I],
KC [auth 1N],
KD [auth 3L],
KE [auth 5J],
LC [auth 2A],
LD [auth 3M],
LE [auth 5K],
MC [auth 2B],
MD [auth 3N],
ME [auth 5L],
NC [auth 2C],
ND [auth 4A],
NE [auth 5M],
OC [auth 2D],
OD [auth 4B],
OE [auth 5N],
PC [auth 2E],
PD [auth 4C],
QC [auth 2F],
QD [auth 4D],
RC [auth 2G],
RD [auth 4E],
SC [auth 2H],
SD [auth 4F],
TC [auth 2I],
TD [auth 4G],
UC [auth 2J],
UD [auth 4H],
VC [auth 2K],
VD [auth 4I],
WC [auth 2L],
WD [auth 4J],
XB [auth 1A],
XC [auth 2M],
XD [auth 4K],
YB [auth 1B],
YC [auth 2N],
YD [auth 4L],
ZB [auth 1C],
ZC [auth 3A],
ZD [auth 4M]
[(2~{S})-3-[[(2~{R})-2,3-bis(oxidanyl)propoxy]-oxidanyl-phosphoryl]oxy-2-hexadec-9-enoyloxy-propyl] hexadecanoate
C38 H73 O10 P
NOFOTAHTYLXZNV-RERZGLEZSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 5.00 Å
  • Aggregation State: HELICAL ARRAY 
  • Reconstruction Method: HELICAL 
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTPHENIX1.10.1-2155
RECONSTRUCTIONIHRSR
RECONSTRUCTIONSPIDER22

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: 2016-11-02
    Type: Initial release
  • Version 1.1: 2017-08-02
    Changes: Data collection
  • Version 1.2: 2017-08-30
    Changes: Data collection
  • Version 1.3: 2018-01-31
    Changes: Data processing