2j9t
From Proteopedia
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|PDB= 2j9t |SIZE=350|CAPTION= <scene name='initialview01'>2j9t</scene>, resolution 2.7Å | |PDB= 2j9t |SIZE=350|CAPTION= <scene name='initialview01'>2j9t</scene>, resolution 2.7Å | ||
|SITE= <scene name='pdbsite=AC1:Bo3+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Bo3+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BO3:BORIC+ACID'>BO3</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j9t OCA], [http://www.ebi.ac.uk/pdbsum/2j9t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j9t RCSB]</span> | ||
}} | }} | ||
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[[Category: Lea, S M.]] | [[Category: Lea, S M.]] | ||
[[Category: Roversi, P.]] | [[Category: Roversi, P.]] | ||
| - | [[Category: BO3]] | ||
| - | [[Category: FLC]] | ||
[[Category: bipd]] | [[Category: bipd]] | ||
[[Category: burkholderia pseudomallei]] | [[Category: burkholderia pseudomallei]] | ||
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[[Category: type 3 secretion system]] | [[Category: type 3 secretion system]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:55:05 2008'' |
Revision as of 00:55, 31 March 2008
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| , resolution 2.7Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. This structure supersedes the now removed PDB entry 2CMQ. 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
Page seeded by OCA on Mon Mar 31 03:55:05 2008
Categories: Burkholderia pseudomallei | Single protein | Deane, J E. | Field, T. | Galyov, E. | Johnson, S. | Lea, S M. | Roversi, P. | Bipd | T3ss | Toxin | Ttss | Type 3 secretion system
