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| | <StructureSection load='2izp' size='340' side='right'caption='[[2izp]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='2izp' size='340' side='right'caption='[[2izp]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2izp]] is a 2 chain structure with sequence from [https://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=2IZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IZP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2izp]] is a 2 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=2IZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IZP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cmq|2cmq]], [[2ixr|2ixr]]</div></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]] 2.1Å</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=2izp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2izp OCA], [https://pdbe.org/2izp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2izp RCSB], [https://www.ebi.ac.uk/pdbsum/2izp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2izp ProSAT]</span></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=2izp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2izp OCA], [https://pdbe.org/2izp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2izp RCSB], [https://www.ebi.ac.uk/pdbsum/2izp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2izp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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>
| + | [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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cooper, J B]] | + | [[Category: Cooper JB]] |
| - | [[Category: Erskine, P T]] | + | [[Category: Erskine PT]] |
| - | [[Category: Fox, G C]] | + | [[Category: Fox GC]] |
| - | [[Category: Gill, R]] | + | [[Category: Gill R]] |
| - | [[Category: Knight, M J]] | + | [[Category: Knight MJ]] |
| - | [[Category: Mikolajek, H]] | + | [[Category: Mikolajek H]] |
| - | [[Category: Ruaux, A]] | + | [[Category: Ruaux A]] |
| - | [[Category: Withers, J]] | + | [[Category: Withers J]] |
| - | [[Category: Wong-Fat-Sang, N]] | + | [[Category: Wong-Fat-Sang N]] |
| - | [[Category: Wood, M]] | + | [[Category: Wood M]] |
| - | [[Category: Wood, S P]] | + | [[Category: Wood SP]] |
| - | [[Category: Invasion protein]]
| + | |
| - | [[Category: Toxin]]
| + | |
| - | [[Category: Type-iii secretion system]]
| + | |
| - | [[Category: Virulence factor]]
| + | |
| 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
Burkoldheria pseudomallei is a Gram-negative bacterium that possesses a protein secretion system similar to those found in Salmonella and Shigella. Recent work has indicated that the protein encoded by the BipD gene of B. pseudomallei is an important secreted virulence factor. BipD is similar in sequence to IpaD from Shigella and SipD from Salmonella and is therefore likely to be a translocator protein in the type-III secretion system of B. pseudomallei. The crystal structure of BipD has been solved at a resolution of 2.1 A revealing the detailed tertiary fold of the molecule. The overall structure is appreciably extended and consists of a bundle of antiparallel alpha-helical segments with two small beta-sheet regions. The longest helices of the molecule form a four-helix bundle and most of the remaining secondary structure elements (three helices and two three-stranded beta-sheets) are formed by the region linking the last two helices of the four-helix bundle. The structure suggests that the biologically active form of the molecule may be a dimer formed by contacts involving the C-terminal alpha-helix, which is the most strongly conserved part of the protein. Comparison of the structure of BipD with immunological and other data for IpaD indicates that the C-terminal alpha-helix is also involved in contacts with other proteins that form the translocon.
High resolution structure of BipD: an invasion protein associated with the type III secretion system of Burkholderia pseudomallei.,Erskine PT, Knight MJ, Ruaux A, Mikolajek H, Wong Fat Sang N, Withers J, Gill R, Wood SP, Wood M, Fox GC, Cooper JB J Mol Biol. 2006 Oct 13;363(1):125-36. Epub 2006 Aug 1. PMID:16950399[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
- ↑ Erskine PT, Knight MJ, Ruaux A, Mikolajek H, Wong Fat Sang N, Withers J, Gill R, Wood SP, Wood M, Fox GC, Cooper JB. High resolution structure of BipD: an invasion protein associated with the type III secretion system of Burkholderia pseudomallei. J Mol Biol. 2006 Oct 13;363(1):125-36. Epub 2006 Aug 1. PMID:16950399 doi:10.1016/j.jmb.2006.07.069
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