2HIL

Structure of the Neisseria gonorrhoeae Type IV pilus filament from x-ray crystallography and electron cryomicroscopy

Summary for 2HIL

• Entry DOI: 10.2210/pdb2hil/pdb
• Related: 2HI2
• EMDB information: 1236
• Descriptor: Fimbrial protein, alpha-D-galactopyranose-(1-3)-2,4-bisacetamido-2,4-dideoxy-beta-D-glucopyranose, PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER (3 entities in total)
• Functional Keywords: type iv pili, virulence factors, dna binding protein, natural transformation, antigenic variation, cell adhesion
• Biological source: Neisseria gonorrhoeae
• Total number of polymer chains: 18
• Total formula weight: 319967.24

Authors

Craig, L.,Volkmann, N.,Egelman, E.H.,Tainer, J.A. (deposition date: 2006-06-29, release date: 2006-09-12, Last modification date: 2025-03-26)

Primary citation

Craig, L.,Volkmann, N.,Arvai, A.S.,Pique, M.E.,Yeager, M.,Egelman, E.H.,Tainer, J.A.
Type IV Pilus Structure by Cryo-Electron Microscopy and Crystallography: Implications for Pilus Assembly and Functions.
Mol.Cell, 23:651-662, 2006

PubMed Abstract: 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.

PubMed: 16949362
DOI: 10.1016/j.molcel.2006.07.004

Experimental method

ELECTRON MICROSCOPY (12.5 Å)