2j9t

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==Overview==
==Overview==
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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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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.
==About this Structure==
==About this Structure==
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2J9T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei] with <scene name='pdbligand=FLC:'>FLC</scene> and <scene name='pdbligand=BO3:'>BO3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 2CMQ. Known structural/functional Site: <scene name='pdbsite=AC1:Bo3+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J9T OCA].
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2J9T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei] with <scene name='pdbligand=FLC:'>FLC</scene> and <scene name='pdbligand=BO3:'>BO3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 2CMQ. Known structural/functional Site: <scene name='pdbsite=AC1:Bo3+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J9T OCA].
==Reference==
==Reference==
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[[Category: Burkholderia pseudomallei]]
[[Category: Burkholderia pseudomallei]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Deane, J.E.]]
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[[Category: Deane, J E.]]
[[Category: Field, T.]]
[[Category: Field, T.]]
[[Category: Galyov, E.]]
[[Category: Galyov, E.]]
[[Category: Johnson, S.]]
[[Category: Johnson, S.]]
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[[Category: Lea, S.M.]]
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[[Category: Lea, S M.]]
[[Category: Roversi, P.]]
[[Category: Roversi, P.]]
[[Category: BO3]]
[[Category: BO3]]
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[[Category: type 3 secretion system]]
[[Category: type 3 secretion system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:43:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:00:50 2008''

Revision as of 16:00, 21 February 2008


2j9t, resolution 2.7Å

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BIPD OF BURKHOLDERIA PSEUDOMALLEI

Overview

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.

About this Structure

2J9T is a Single protein structure of sequence from Burkholderia pseudomallei with and as ligands. This structure supersedes the now removed PDB entry 2CMQ. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD., Johnson S, Roversi P, Espina M, Olive A, Deane JE, Birket S, Field T, Picking WD, Blocker AJ, Galyov EE, Picking WL, Lea SM, J Biol Chem. 2007 Feb 9;282(6):4035-44. Epub 2006 Oct 31. PMID:17077085

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