2ixr: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ixr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IXR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IXR FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ixr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IXR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IXR FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cmq|2cmq]], [[2izp|2izp]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cmq|2cmq]], [[2izp|2izp]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ixr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ixr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ixr RCSB], [http://www.ebi.ac.uk/pdbsum/2ixr PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ixr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ixr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ixr RCSB], [http://www.ebi.ac.uk/pdbsum/2ixr PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 29: | Line 29: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Burkholderia pseudomallei]] | [[Category: Burkholderia pseudomallei]] | ||
[[Category: Deane, J E | [[Category: Deane, J E]] | ||
[[Category: Field, T | [[Category: Field, T]] | ||
[[Category: Galyov, E E | [[Category: Galyov, E E]] | ||
[[Category: Johnson, S | [[Category: Johnson, S]] | ||
[[Category: Lea, S M | [[Category: Lea, S M]] | ||
[[Category: Roversi, P | [[Category: Roversi, P]] | ||
[[Category: Bipd]] | [[Category: Bipd]] | ||
[[Category: T3ss]] | [[Category: T3ss]] | ||
[[Category: Toxin]] | [[Category: Toxin]] | ||
[[Category: Ttss]] | [[Category: Ttss]] | ||
[[Category: Type 3 secretion system]] | [[Category: Type 3 secretion system]] | ||
Revision as of 19:53, 19 January 2015
BIPD OF BURKHOLDERIA PSEUDOMALLEIBIPD OF BURKHOLDERIA PSEUDOMALLEI
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBacteria 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||