2opd: Difference between revisions

Revision as of 19:21, 21 February 2008

Structure of the Neisseria meningitidis minor Type IV pilin, PilX

OverviewOverview

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.

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 Thu Feb 21 18:21:03 2008

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 ==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.
+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.
 ==About this Structure==
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 [[Category: Neisseria meningitidis]]
 [[Category: Single protein]]
-[[Category: Dyer, D.H.]]
+[[Category: Dyer, D H.]]
-[[Category: Forest, K.T.]]
+[[Category: Forest, K T.]]
 [[Category: Helaine, S.]]
 [[Category: Pelicic, V.]]
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 [[Category: type iv pilin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:43:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:21:03 2008''