Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD.

Bacteria expressing type III secretion systems (T3SS) have been responsible for the deaths of millions worldwide, acting as key virulence elements in diseases ranging from plague to typhoid fever. The T3SS is composed of a basal body, which traverses both bacterial membranes, and an external needle...

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Main Authors: Johnson, S, Roversi, P, Espina, M, Olive, A, Deane, J, Birket, S, Field, T, Picking, W, Blocker, A, Galyov, E, Lea, S
Format: Journal article
Language:English
Published: 2007
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author Johnson, S
Roversi, P
Espina, M
Olive, A
Deane, J
Birket, S
Field, T
Picking, W
Blocker, A
Galyov, E
Picking, W
Lea, S
author_facet Johnson, S
Roversi, P
Espina, M
Olive, A
Deane, J
Birket, S
Field, T
Picking, W
Blocker, A
Galyov, E
Picking, W
Lea, S
author_sort Johnson, S
collection OXFORD
description Bacteria expressing type III secretion systems (T3SS) have been responsible for the deaths of millions worldwide, acting as key virulence elements in diseases ranging from plague to typhoid fever. The T3SS is composed of a basal body, which traverses both bacterial membranes, and an external needle through which effector proteins are secreted. We report multiple crystal structures of two proteins that sit at the tip of the needle and are essential for virulence: IpaD from Shigella flexneri and BipD from Burkholderia pseudomallei. The structures reveal that the N-terminal domains of the molecules are intramolecular chaperones that prevent premature oligomerization, as well as sharing structural homology with proteins involved in eukaryotic actin rearrangement. Crystal packing has allowed us to construct a model for the tip complex that is supported by mutations designed using the structure.
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spelling oxford-uuid:0cbb19e6-73f0-4583-8259-360b7fbdb1282022-03-26T09:36:33ZSelf-chaperoning of the type III secretion system needle tip proteins IpaD and BipD.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:0cbb19e6-73f0-4583-8259-360b7fbdb128EnglishSymplectic Elements at Oxford2007Johnson, SRoversi, PEspina, MOlive, ADeane, JBirket, SField, TPicking, WBlocker, AGalyov, EPicking, WLea, SBacteria expressing type III secretion systems (T3SS) have been responsible for the deaths of millions worldwide, acting as key virulence elements in diseases ranging from plague to typhoid fever. The T3SS is composed of a basal body, which traverses both bacterial membranes, and an external needle through which effector proteins are secreted. We report multiple crystal structures of two proteins that sit at the tip of the needle and are essential for virulence: IpaD from Shigella flexneri and BipD from Burkholderia pseudomallei. The structures reveal that the N-terminal domains of the molecules are intramolecular chaperones that prevent premature oligomerization, as well as sharing structural homology with proteins involved in eukaryotic actin rearrangement. Crystal packing has allowed us to construct a model for the tip complex that is supported by mutations designed using the structure.
spellingShingle Johnson, S
Roversi, P
Espina, M
Olive, A
Deane, J
Birket, S
Field, T
Picking, W
Blocker, A
Galyov, E
Picking, W
Lea, S
Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD.
title Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD.
title_full Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD.
title_fullStr Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD.
title_full_unstemmed Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD.
title_short Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD.
title_sort self chaperoning of the type iii secretion system needle tip proteins ipad and bipd
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