2jaa: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:2jaa.jpg|left|200px]] | [[Image:2jaa.jpg|left|200px]] | ||
'''SEMET SUBSTITUTED SHIGELLA FLEXNERI IPAD''' | {{Structure | ||
|PDB= 2jaa |SIZE=350|CAPTION= <scene name='initialview01'>2jaa</scene>, resolution 3.1Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SEMET SUBSTITUTED SHIGELLA FLEXNERI IPAD''' | |||
==Overview== | ==Overview== | ||
Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
2JAA is a [ | 2JAA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JAA OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17077085 17077085] | ||
[[Category: Shigella flexneri]] | [[Category: Shigella flexneri]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Line 35: | Line 44: | ||
[[Category: virulence]] | [[Category: virulence]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:39:19 2008'' |
Revision as of 18:39, 20 March 2008
| |||||||
, resolution 3.1Å | |||||||
---|---|---|---|---|---|---|---|
Coordinates: | save as pdb, mmCIF, xml |
SEMET SUBSTITUTED SHIGELLA FLEXNERI IPAD
OverviewOverview
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 StructureAbout this Structure
2JAA is a Single protein structure of sequence from Shigella flexneri. Full crystallographic information is available from OCA.
ReferenceReference
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 Thu Mar 20 17:39:19 2008