7JSV

Cryo-EM structure of conjugative pili from carbapenem-resistant Klebsiella pneumoniae


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.90 Å
  • Aggregation State: FILAMENT 
  • Reconstruction Method: HELICAL 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Cryoelectron-Microscopic Structure of the pKpQIL Conjugative Pili from Carbapenem-Resistant Klebsiella pneumoniae.

Zheng, W.Pena, A.Low, W.W.Wong, J.L.C.Frankel, G.Egelman, E.H.

(2020) Structure 28: 1321

  • DOI: https://doi.org/10.1016/j.str.2020.08.010
  • Primary Citation of Related Structures:  
    7JSV

  • PubMed Abstract: 

    Conjugative pili are important in mediating bacterial conjugation and horizontal gene transfer. Since plasmid transfer can include antibiotic-resistance genes, conjugation is an important mechanism in the spread of antibiotic resistance. Filamentous bacteriophages have been shown to exist in two different structural classes: those with a 5-fold rotational symmetry and those with a one-start helix with approximately 5 subunits per turn. Structures for the F and the F-like pED208 conjugation pilus have shown that they have 5-fold rotational symmetry. Here, we report the cryoelectron-microscopic structure of conjugative pili from carbapenem-resistant Klebsiella pneumoniae, encoded on the IncFIIK pKpQIL plasmid, at 3.9 Å resolution and show that it has a one-start helix. These results establish that conjugation pili can exist in at least two structural classes, consistent with other results showing that relatively small perturbations are needed to change the helical symmetry of polymers.


  • Organizational Affiliation

    Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22903, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Pilin69Klebsiella pneumoniaeMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for A6TIG0 (Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578))
Explore A6TIG0 
Go to UniProtKB:  A6TIG0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA6TIG0
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
LHG
Query on LHG

Download Ideal Coordinates CCD File 
AB [auth L]
AC [auth l]
BB [auth M]
BC [auth m]
CB [auth N]
AB [auth L],
AC [auth l],
BB [auth M],
BC [auth m],
CB [auth N],
CC [auth n],
DB [auth O],
DC [auth o],
EB [auth P],
FB [auth Q],
GB [auth R],
HB [auth S],
IB [auth T],
JB [auth U],
KB [auth V],
LB [auth W],
MB [auth X],
NB [auth Y],
OB [auth Z],
PA [auth A],
PB [auth a],
QA [auth B],
QB [auth b],
RA [auth C],
RB [auth c],
SA [auth D],
SB [auth d],
TA [auth E],
TB [auth e],
UA [auth F],
UB [auth f],
VA [auth G],
VB [auth g],
WA [auth H],
WB [auth h],
XA [auth I],
XB [auth i],
YA [auth J],
YB [auth j],
ZA [auth K],
ZB [auth k]
1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE
C38 H75 O10 P
BIABMEZBCHDPBV-MPQUPPDSSA-N
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.90 Å
  • Aggregation State: FILAMENT 
  • Reconstruction Method: HELICAL 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION
MODEL REFINEMENTCoot
MODEL REFINEMENTPHENIX

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)United StatesR35GM122510

Revision History  (Full details and data files)

  • Version 1.0: 2020-09-02
    Type: Initial release
  • Version 1.1: 2020-09-23
    Changes: Database references
  • Version 1.2: 2020-12-16
    Changes: Database references
  • Version 1.3: 2024-03-06
    Changes: Data collection, Database references