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TitleType IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions.
Journal, issue, pagesMol Cell, Vol. 23, Issue 5, Page 651-662, Year 2006
Publish dateSep 1, 2006
AuthorsLisa Craig / Niels Volkmann / Andrew S Arvai / Michael E Pique / Mark Yeager / Edward H Egelman / John A Tainer /
PubMed AbstractType IV pili (T4P) are long, thin, flexible filaments on bacteria that undergo assembly-disassembly from inner membrane pilin subunits and exhibit astonishing multifunctionality. Neisseria ...Type IV pili (T4P) are long, thin, flexible filaments on bacteria that undergo assembly-disassembly from inner membrane pilin subunits and exhibit astonishing multifunctionality. Neisseria gonorrhoeae (gonococcal or GC) T4P are prototypic virulence factors and immune targets for increasingly antibiotic-resistant human pathogens, yet detailed structures are unavailable for any T4P. Here, we determined a detailed experimental GC-T4P structure by quantitative fitting of a 2.3 A full-length pilin crystal structure into a 12.5 A resolution native GC-T4P reconstruction solved by cryo-electron microscopy (cryo-EM) and iterative helical real space reconstruction. Spiraling three-helix bundles form the filament core, anchor the globular heads, and provide strength and flexibility. Protruding hypervariable loops and posttranslational modifications in the globular head shield conserved functional residues in pronounced grooves, creating a surprisingly corrugated pilus surface. These results clarify T4P multifunctionality and assembly-disassembly while suggesting unified assembly mechanisms for T4P, archaeal flagella, and type II secretion system filaments.
External linksMol Cell / PubMed:16949362
MethodsEM (helical sym.) / X-ray diffraction
Resolution2.3 - 12.5 Å
Structure data

1236

2hil

EMDB-1236: Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions.
PDB-2hil: Structure of the Neisseria gonorrhoeae Type IV pilus filament from x-ray crystallography and electron cryomicroscopy
Method: EM (helical sym.) / Resolution: 12.5 Å

PDB-2hi2:
Crystal structure of native Neisseria gonorrhoeae Type IV pilin at 2.3 Angstroms Resolution
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-HTO:
HEPTANE-1,2,3-TRIOL

ChemComp-OPE:
PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER / Phosphorylethanolamine

ChemComp-HOH:
WATER / Water

Source
  • neisseria gonorrhoeae (bacteria)
KeywordsCELL ADHESION / TYPE IV PILIN / FIBER-FORMING PROTEIN / membrane protein / DNA binding protein / contractile protein / TYPE IV PILI / virulence factors / natural transformation / antigenic variation

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