2hi2
From Proteopedia
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Crystal structure of native Neisseria gonorrhoeae Type IV pilin at 2.3 Angstroms Resolution
Overview
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.
About this Structure
2HI2 is a Single protein structure of sequence from Neisseria gonorrhoeae with HTO and OPE as ligands. Full crystallographic information is available from OCA.
Reference
Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions., Craig L, Volkmann N, Arvai AS, Pique ME, Yeager M, Egelman EH, Tainer JA, Mol Cell. 2006 Sep 1;23(5):651-62. PMID:16949362
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