2jaa

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[[Image:2jaa.jpg|left|200px]]
 
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==SeMet substituted Shigella Flexneri Ipad==
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The line below this paragraph, containing "STRUCTURE_2jaa", creates the "Structure Box" on the page.
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<StructureSection load='2jaa' size='340' side='right'caption='[[2jaa]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2jaa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JAA FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2j0n|2j0n]], [[2j0o|2j0o]]</div></td></tr>
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{{STRUCTURE_2jaa| PDB=2jaa | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jaa OCA], [https://pdbe.org/2jaa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jaa RCSB], [https://www.ebi.ac.uk/pdbsum/2jaa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jaa ProSAT]</span></td></tr>
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</table>
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'''SEMET SUBSTITUTED SHIGELLA FLEXNERI IPAD'''
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== Function ==
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[[https://www.uniprot.org/uniprot/IPAD_SHIFL IPAD_SHIFL]] Required for bacterial invasion of host cells. Controls IpaB and IpaC secretion, and the efficiency with which they are physically inserted into target cell membranes. These proteins are exported via TTSS to form a pore in the host membrane that allows the translocation of the other effectors into the host cytoplasm. Along with IpaB, is essential for both blocking secretion through the Mxi/Spa translocon in the absence of a secretion-inducing signal, and for controlling the level of secretion in the presence of this signal.<ref>PMID:7957095</ref> <ref>PMID:15731041</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ja/2jaa_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2jaa ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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>
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2JAA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JAA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://www.ncbi.nlm.nih.gov/pubmed/17077085 17077085]
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</div>
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[[Category: Shigella flexneri]]
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<div class="pdbe-citations 2jaa" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Birket, S.]]
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<references/>
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[[Category: Blocker, A.]]
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__TOC__
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[[Category: Deane, J E.]]
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</StructureSection>
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[[Category: Espina, M.]]
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[[Category: Large Structures]]
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[[Category: Field, T.]]
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[[Category: Birket, S]]
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[[Category: Galyov, E E.]]
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[[Category: Blocker, A J]]
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[[Category: Johnson, S.]]
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[[Category: Deane, J E]]
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[[Category: Lea, S M.]]
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[[Category: Espina, M]]
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[[Category: Olive, A.]]
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[[Category: Field, T]]
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[[Category: Picking, W D.]]
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[[Category: Galyov, E E]]
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[[Category: Picking, W L.]]
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[[Category: Johnson, S]]
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[[Category: Roversi, P.]]
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[[Category: Lea, S M]]
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[[Category: Olive, A]]
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[[Category: Picking, W D]]
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[[Category: Picking, W L]]
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[[Category: Roversi, P]]
[[Category: Cell invasion]]
[[Category: Cell invasion]]
[[Category: Invasin]]
[[Category: Invasin]]
[[Category: Ipad]]
[[Category: Ipad]]
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[[Category: Plasmid]]
 
[[Category: Semet]]
[[Category: Semet]]
[[Category: Shigella flexneri]]
[[Category: Shigella flexneri]]
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[[Category: Type iii secretion]]
[[Category: Type iii secretion]]
[[Category: Virulence]]
[[Category: Virulence]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:35:50 2008''
 

Current revision

SeMet substituted Shigella Flexneri Ipad

PDB ID 2jaa

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