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==Structure of the Neisseria meningitidis minor Type IV pilin, PilX== | |||
<StructureSection load='2opd' size='340' side='right'caption='[[2opd]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2opd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OPD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=2opd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2opd OCA], [https://pdbe.org/2opd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2opd RCSB], [https://www.ebi.ac.uk/pdbsum/2opd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2opd ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Type IV pili (Tfp) are widespread filamentous bacterial organelles that mediate multiple virulence-related phenotypes. They are composed mainly of pilin subunits, which are processed before filament assembly by dedicated prepilin peptidases. Other proteins processed by these peptidases, whose molecular nature and mode of action remain enigmatic, play critical roles in Tfp biology. We have performed a detailed structure/function analysis of one such protein, PilX from Neisseria meningitidis, which is crucial for formation of bacterial aggregates and adhesion to human cells. The x-ray crystal structure of PilX reveals the alpha/beta roll fold shared by all pilins, and we show that this protein colocalizes with Tfp. These observations suggest that PilX is a minor, or low abundance, pilin that assembles within the filaments in a similar way to pilin. Deletion of a PilX distinctive structural element, which is predicted to be exposed on the filament surface, abolishes aggregation and adhesion. Our results support a model in which surface-exposed motifs in PilX subunits stabilize bacterial aggregates against the disruptive force of pilus retraction and illustrate how a minor pilus component can enhance the functional properties of pili of rather simple composition and structure. | |||
3D structure/function analysis of PilX reveals how minor pilins can modulate the virulence properties of type IV pili.,Helaine S, Dyer DH, Nassif X, Pelicic V, Forest KT Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15888-93. Epub 2007 Sep 24. PMID:17893339<ref>PMID:17893339</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2opd" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Pilin 3D structures|Pilin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Neisseria meningitidis]] | [[Category: Neisseria meningitidis]] | ||
[[Category: Dyer DH]] | |||
[[Category: Dyer | [[Category: Forest KT]] | ||
[[Category: Forest | [[Category: Helaine S]] | ||
[[Category: Helaine | [[Category: Pelicic V]] | ||
[[Category: Pelicic | |||
Latest revision as of 04:16, 21 November 2024
Structure of the Neisseria meningitidis minor Type IV pilin, PilXStructure of the Neisseria meningitidis minor Type IV pilin, PilX
Structural highlights
Publication Abstract from PubMedType IV pili (Tfp) are widespread filamentous bacterial organelles that mediate multiple virulence-related phenotypes. They are composed mainly of pilin subunits, which are processed before filament assembly by dedicated prepilin peptidases. Other proteins processed by these peptidases, whose molecular nature and mode of action remain enigmatic, play critical roles in Tfp biology. We have performed a detailed structure/function analysis of one such protein, PilX from Neisseria meningitidis, which is crucial for formation of bacterial aggregates and adhesion to human cells. The x-ray crystal structure of PilX reveals the alpha/beta roll fold shared by all pilins, and we show that this protein colocalizes with Tfp. These observations suggest that PilX is a minor, or low abundance, pilin that assembles within the filaments in a similar way to pilin. Deletion of a PilX distinctive structural element, which is predicted to be exposed on the filament surface, abolishes aggregation and adhesion. Our results support a model in which surface-exposed motifs in PilX subunits stabilize bacterial aggregates against the disruptive force of pilus retraction and illustrate how a minor pilus component can enhance the functional properties of pili of rather simple composition and structure. 3D structure/function analysis of PilX reveals how minor pilins can modulate the virulence properties of type IV pili.,Helaine S, Dyer DH, Nassif X, Pelicic V, Forest KT Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15888-93. Epub 2007 Sep 24. PMID:17893339[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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