View source for 5vxx


==Cryo-EM reconstruction of Neisseria gonorrhoeae Type IV pilus==
<SX load='5vxx' size='340' side='right' viewer='molstar' caption='[[5vxx]], [[Resolution|resolution]] 5.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vxx]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VXX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B6D:2,4-BIS(ACETYLAMINO)-2,4,6-TRIDEOXY-BETA-D-GLUCOPYRANOSE'>B6D</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=OPE:PHOSPHORIC+ACID+MONO-(2-AMINO-ETHYL)+ESTER'>OPE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5vxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vxx OCA], [https://pdbe.org/5vxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vxx RCSB], [https://www.ebi.ac.uk/pdbsum/5vxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vxx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FMM1_NEIGO FMM1_NEIGO] This protein is the predominant Neisseria surface antigen, which allows adhesion of the bacterium to various host cells.
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== Publication Abstract from PubMed ==
We report here cryoelectron microscopy reconstructions of type IV pili (T4P) from two important human pathogens, Pseudomonas aeruginosa and Neisseria gonorrhoeae, at approximately 8 and 5 A resolution, respectively. The two structures reveal distinct arrangements of the pilin globular domains on the pilus surfaces, which impart different helical parameters, but similar packing of the conserved N-terminal alpha helices, alpha1, in the filament core. In contrast to the continuous alpha helix seen in the X-ray crystal structures of the P. aeruginosa and N. gonorrhoeae pilin subunits, alpha1 in the pilus filaments has a melted segment located between conserved helix-breaking residues Gly14 and Pro22, as seen for the Neisseria meningitidis T4P. Using mutagenesis we show that Pro22 is critical for pilus assembly, as are Thr2 and Glu5, which are positioned to interact in the hydrophobic filament core. These structures provide a framework for understanding T4P assembly, function, and biophysical properties.

Cryoelectron Microscopy Reconstructions of the Pseudomonas aeruginosa and Neisseria gonorrhoeae Type IV Pili at Sub-nanometer Resolution.,Wang F, Coureuil M, Osinski T, Orlova A, Altindal T, Gesbert G, Nassif X, Egelman EH, Craig L Structure. 2017 Sep 5;25(9):1423-1435.e4. doi: 10.1016/j.str.2017.07.016. PMID:28877506<ref>PMID:28877506</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5vxx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pilin 3D structures|Pilin 3D structures]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Neisseria gonorrhoeae]]
[[Category: Altindal T]]
[[Category: Craig L]]
[[Category: Egelman EH]]
[[Category: Orlova A]]
[[Category: Wang F]]