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5LEG

Structure of the bacterial sex F pilus (pED208)

This is a non-PDB format compatible entry.
Summary for 5LEG
Entry DOI10.2210/pdb5leg/pdb
EMDB information4042
DescriptorPilin, 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE (2 entities in total)
Functional Keywordsf-pilus conjugation type iv secretion system phospholipid, protein fibril
Biological sourceSalmonella enterica subsp. enterica serovar Typhi
Cellular locationCell inner membrane; Multi-pass membrane protein: P12060
Total number of polymer chains80
Total formula weight594242.75
Authors
Costa, T.R.D.,Ilangovan, I.,Ukleja, M.,Redzej, A.,Santini, J.M.,Smith, T.K.,Egelman, E.H.,Waksman, G. (deposition date: 2016-06-29, release date: 2016-09-28, Last modification date: 2024-05-15)
Primary citationCosta, T.R.,Ilangovan, A.,Ukleja, M.,Redzej, A.,Santini, J.M.,Smith, T.K.,Egelman, E.H.,Waksman, G.
Structure of the Bacterial Sex F Pilus Reveals an Assembly of a Stoichiometric Protein-Phospholipid Complex.
Cell, 166:1436-1444.e10, 2016
Cited by
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.
PubMed: 27610568
DOI: 10.1016/j.cell.2016.08.025
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

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