2opd: Difference between revisions

Revision as of 16:03, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2opd.png

Template:STRUCTURE 2opd

Structure of the Neisseria meningitidis minor Type IV pilin, PilXStructure of the Neisseria meningitidis minor Type IV pilin, PilX

Template:ABSTRACT PUBMED 17893339

About this StructureAbout this Structure

2OPD is a Single protein structure of sequence from Neisseria meningitidis. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 16:03:46 2008

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OCA

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-'''Structure of the Neisseria meningitidis minor Type IV pilin, PilX'''
+===Structure of the Neisseria meningitidis minor Type IV pilin, PilX===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17893339}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17893339 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17893339}}
 ==About this Structure==
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 [[Category: Pilx]]
 [[Category: Type iv pilin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:22:54 2008''
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