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| | ==Near-atomic resolution analysis of BipD- A component of the type-III secretion system of Burkholderia pseudomallei== | | ==Near-atomic resolution analysis of BipD- A component of the type-III secretion system of Burkholderia pseudomallei== |
| - | <StructureSection load='3nft' size='340' side='right' caption='[[3nft]], [[Resolution|resolution]] 1.51Å' scene=''> | + | <StructureSection load='3nft' size='340' side='right'caption='[[3nft]], [[Resolution|resolution]] 1.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nft]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pseudomallei"_whitmore_1913 "bacillus pseudomallei" whitmore 1913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NFT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nft]] 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=3NFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NFT FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2izp|2izp]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.51Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bipD, BPSS1529 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 "Bacillus pseudomallei" Whitmore 1913])</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=3nft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nft OCA], [https://pdbe.org/3nft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nft RCSB], [https://www.ebi.ac.uk/pdbsum/3nft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nft ProSAT]</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=3nft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nft OCA], [http://pdbe.org/3nft PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nft RCSB], [http://www.ebi.ac.uk/pdbsum/3nft PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nft ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus pseudomallei whitmore 1913]] | + | [[Category: Burkholderia pseudomallei]] |
| - | [[Category: Cooper, J B]] | + | [[Category: Large Structures]] |
| - | [[Category: Erskine, P T]] | + | [[Category: Cooper JB]] |
| - | [[Category: Gill, R S]] | + | [[Category: Erskine PT]] |
| - | [[Category: Pal, M]] | + | [[Category: Gill RS]] |
| - | [[Category: Wood, S P]] | + | [[Category: Pal M]] |
| - | [[Category: Translocation]] | + | [[Category: Wood SP]] |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Virulence]]
| + | |
| Structural highlights
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
Burkholderia pseudomallei, the causative agent of melioidosis, possesses a type III protein secretion apparatus that is similar to those found in Salmonella and Shigella. A major function of these secretion systems is to inject virulence-associated proteins into target cells of the host organism. The bipD gene of B. pseudomallei encodes a secreted virulence factor that is similar in sequence and is most likely to be functionally analogous to IpaD from Shigella and SipD from Salmonella. Proteins in this family are thought to act as extracellular chaperones at the tip of the secretion needle to help the hydrophobic translocator proteins enter the target cell membrane, where they form a pore and may also link the translocon pore with the secretion needle. BipD has been crystallized in a monoclinic crystal form that diffracted X-rays to 1.5 A resolution and the structure was refined to an R factor of 16.1% and an Rfree of 19.8% at this resolution. The putative dimer interface that was observed in previous crystal structures was retained and a larger surface area was buried in the new crystal form.
Near-atomic resolution analysis of BipD, a component of the type III secretion system of Burkholderia pseudomallei.,Pal M, Erskine PT, Gill RS, Wood SP, Cooper JB Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt, 9):990-3. Epub 2010 Aug 21. PMID:20823511[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
- ↑ Pal M, Erskine PT, Gill RS, Wood SP, Cooper JB. Near-atomic resolution analysis of BipD, a component of the type III secretion system of Burkholderia pseudomallei. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt, 9):990-3. Epub 2010 Aug 21. PMID:20823511 doi:10.1107/S1744309110026333
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