2hil: Difference between revisions
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'''Structure of the Neisseria gonorrhoeae Type IV pilus filament from x-ray crystallography and electron cryomicroscopy''' | '''Structure of the Neisseria gonorrhoeae Type IV pilus filament from x-ray crystallography and electron cryomicroscopy''' | ||
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==About this Structure== | ==About this Structure== | ||
2HIL is a [[Single protein]] structure | 2HIL is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIL OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Volkmann, N.]] | [[Category: Volkmann, N.]] | ||
[[Category: 3d image reconstruction]] | [[Category: 3d image reconstruction]] | ||
[[Category: | [[Category: Antigenic variation]] | ||
[[Category: | [[Category: Dna binding protein]] | ||
[[Category: | [[Category: Electron cryomicroscopy]] | ||
[[Category: | [[Category: Natural transformation]] | ||
[[Category: | [[Category: Type iv pili]] | ||
[[Category: | [[Category: Virulence factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:20:15 2008'' | |||
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Revision as of 06:20, 4 May 2008
Structure of the Neisseria gonorrhoeae Type IV pilus filament from x-ray crystallography and electron cryomicroscopy
OverviewOverview
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 StructureAbout this Structure
2HIL is a Single protein structure. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sun May 4 06:20:15 2008