1oqv

<table><tr><td colspan='2'>[[1oqv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OQV FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1oqw|1oqw]], [[1or9|1or9]], [[1dzo|1dzo]], [[2pil|2pil]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tcpa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 "Bacillo virgola del Koch" Trevisan 1884])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1oqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oqv OCA], [http://pdbe.org/1oqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oqv RCSB], [http://www.ebi.ac.uk/pdbsum/1oqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oqv ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/TCPA_VIBCL TCPA_VIBCL]] Constituent of pili, which may be involved in adhesion of V.cholerae to the host intestinal epithelium.

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== Publication Abstract from PubMed ==

Pilin assembly into type IV pili is required for virulence by bacterial pathogens that cause diseases such as cholera, pneumonia, gonorrhea, and meningitis. Crystal structures of soluble, N-terminally truncated pilin from Vibrio cholera toxin-coregulated pilus (TCP) and full-length PAK pilin from Pseudomonas aeruginosa reveal a novel TCP fold, yet a shared architecture for the type IV pilins. In each pilin subunit a conserved, extended, N-terminal alpha helix wrapped by beta strands anchors the structurally variable globular head. Inside the assembled pilus, characterized by cryo-electron microscopy and crystallography, the extended hydrophobic alpha helices make multisubunit contacts to provide mechanical strength and flexibility. Outside, distinct interactions of adaptable heads contribute surface variation for specificity of pilus function in antigenicity, motility, adhesion, and colony formation.

 

== References ==

[[Category: Bacillo virgola del koch trevisan 1884]]

[[Category: Craig, L]]

[[Category: Tainer, J A]]

[[Category: Adhesin]]

[[Category: Cell adhesion]]

[[Category: Fiber forming protein]]

[[Category: Fimbriae]]

[[Category: Pilin]]

[[Category: Pilus filament]]

[[Category: Tcpa]]

[[Category: Type iv pilin]]