2ixr

From Proteopedia

(Difference between revisions)

Current revision

BipD of Burkholderia Pseudomallei

Structural highlights

2ixr is a 1 chain structure with sequence from Burkholderia pseudomallei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BIPD_BURPS Required for invasion of epithelial cells, as well as for survival within host cells, escape from endocytic vesicles and subsequent actin-tail formation. Probably regulates the secretion of effectors BipB and BipC and their final integration into the target cell membrane.^[1] ^[2]

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 PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Stevens MP, Wood MW, Taylor LA, Monaghan P, Hawes P, Jones PW, Wallis TS, Galyov EE. An Inv/Mxi-Spa-like type III protein secretion system in Burkholderia pseudomallei modulates intracellular behaviour of the pathogen. Mol Microbiol. 2002 Nov;46(3):649-59. PMID:12410823
↑ Stevens MP, Haque A, Atkins T, Hill J, Wood MW, Easton A, Nelson M, Underwood-Fowler C, Titball RW, Bancroft GJ, Galyov EE. Attenuated virulence and protective efficacy of a Burkholderia pseudomallei bsa type III secretion mutant in murine models of melioidosis. Microbiology. 2004 Aug;150(Pt 8):2669-76. PMID:15289563 doi:10.1099/mic.0.27146-0
↑ Johnson S, Roversi P, Espina M, Olive A, Deane JE, Birket S, Field T, Picking WD, Blocker AJ, Galyov EE, Picking WL, Lea SM. Self-chaperoning of the type III secretion system needle tip proteins IpaD and BipD. J Biol Chem. 2007 Feb 9;282(6):4035-44. Epub 2006 Oct 31. PMID:17077085 doi:10.1074/jbc.M607945200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ixr"

@@ Line 1: / Line 1: @@
-[[Image:2ixr.jpg|left|200px]]<br /><applet load="2ixr" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2ixr, resolution 2.6&Aring;" />
-'''BIPD OF BURKHOLDERIA PSEUDOMALLEI'''<br />
-==Overview==
+==BipD of Burkholderia Pseudomallei==
-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.
+<StructureSection load='2ixr' size='340' side='right'caption='[[2ixr]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2ixr]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2IXR FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ixr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ixr OCA], [https://pdbe.org/2ixr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ixr RCSB], [https://www.ebi.ac.uk/pdbsum/2ixr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ixr ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/BIPD_BURPS BIPD_BURPS] Required for invasion of epithelial cells, as well as for survival within host cells, escape from endocytic vesicles and subsequent actin-tail formation. Probably regulates the secretion of effectors BipB and BipC and their final integration into the target cell membrane.<ref>PMID:12410823</ref> <ref>PMID:15289563</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/2ixr_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ixr ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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==
+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<ref>PMID:17077085</ref>
-IXR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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://ispc.weizmann.ac.il//pmbin/getpm?pmid=17077085 17077085]
+</div>
+<div class="pdbe-citations 2ixr" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Burkholderia pseudomallei]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Deane, J.E.]]
+[[Category: Deane JE]]
-[[Category: Field, T.]]
+[[Category: Field T]]
-[[Category: Galyov, E.E.]]
+[[Category: Galyov EE]]
-[[Category: Johnson, S.]]
+[[Category: Johnson S]]
-[[Category: Lea, S.M.]]
+[[Category: Lea SM]]
-[[Category: Roversi, P.]]
+[[Category: Roversi P]]
-[[Category: bipd]]
-[[Category: burkholderia pseudomallei]]
-[[Category: t3ss]]
-[[Category: toxin]]
-[[Category: ttss]]
-[[Category: type 3 secretion system]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:48:10 2008''

2ixr

From Proteopedia

Current revision

BipD of Burkholderia Pseudomallei

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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