2HI2

Crystal structure of native Neisseria gonorrhoeae Type IV pilin at 2.3 Angstroms Resolution

Summary for 2HI2

• Entry DOI: 10.2210/pdb2hi2/pdb
• Related: 2HIL
• EMDB information: 1236
• Descriptor: Fimbrial protein, alpha-D-galactopyranose-(1-3)-2,4-bisacetamido-2,4-dideoxy-beta-D-glucopyranose, HEPTANE-1,2,3-TRIOL, ... (5 entities in total)
• Functional Keywords: type iv pilin, fiber-forming protein, membrane protein, dna binding protein, contractile protein, cell adhesion
• Biological source: Neisseria gonorrhoeae
• Total number of polymer chains: 1
• Total formula weight: 17924.16

Authors

Craig, L.,Arvai, A.S.,Tainer, J.A. (deposition date: 2006-06-28, release date: 2006-09-12, Last modification date: 2023-08-30)

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

X-RAY DIFFRACTION (2.3 Å)