2j9t: Difference between revisions
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<StructureSection load='2j9t' size='340' side='right'caption='[[2j9t]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='2j9t' size='340' side='right'caption='[[2j9t]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2j9t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2j9t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2cmq 2cmq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J9T FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BO3:BORIC+ACID'>BO3</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></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=2j9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j9t OCA], [https://pdbe.org/2j9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j9t RCSB], [https://www.ebi.ac.uk/pdbsum/2j9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j9t 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=2j9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j9t OCA], [https://pdbe.org/2j9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j9t RCSB], [https://www.ebi.ac.uk/pdbsum/2j9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j9t ProSAT]</span></td></tr> | ||
</table> | </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 == | == 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: | [[Category: Burkholderia pseudomallei]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Deane | [[Category: Deane JE]] | ||
[[Category: Field | [[Category: Field T]] | ||
[[Category: Galyov | [[Category: Galyov E]] | ||
[[Category: Johnson | [[Category: Johnson S]] | ||
[[Category: Lea | [[Category: Lea SM]] | ||
[[Category: Roversi | [[Category: Roversi P]] | ||
Latest revision as of 12:35, 9 May 2024
BipD of Burkholderia PseudomalleiBipD of Burkholderia Pseudomallei
Structural highlights
FunctionBIPD_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 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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