2hil: Difference between revisions

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[[Image:2hil.gif|left|200px]]<br /><applet load="2hil" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2hil.gif|left|200px]]
caption="2hil, resolution 12.5&Aring;" />
 
'''Structure of the Neisseria gonorrhoeae Type IV pilus filament from x-ray crystallography and electron cryomicroscopy'''<br />
{{Structure
|PDB= 2hil |SIZE=350|CAPTION= <scene name='initialview01'>2hil</scene>, resolution 12.5&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=OPE:PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER'>OPE</scene>
|ACTIVITY=
|GENE=
}}
 
'''Structure of the Neisseria gonorrhoeae Type IV pilus filament from x-ray crystallography and electron cryomicroscopy'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2HIL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=OPE:'>OPE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIL OCA].  
2HIL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIL OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16949362 16949362]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16949362 16949362]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Craig, L.]]
[[Category: Craig, L.]]
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[[Category: natural transformation]]
[[Category: natural transformation]]
[[Category: type iv pili]]
[[Category: type iv pili]]
[[Category: virulence factors]]
[[Category: virulence factor]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:42:16 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:17:33 2008''

Revision as of 18:17, 20 March 2008

File:2hil.gif


PDB ID 2hil

Drag the structure with the mouse to rotate
, resolution 12.5Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



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 of sequence from [1]. 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

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