3f4s

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{{Seed}}
 
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[[Image:3f4s.png|left|200px]]
 
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==Crystal structure of Wolbachia pipientis alpha-DsbA1 T172V==
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The line below this paragraph, containing "STRUCTURE_3f4s", creates the "Structure Box" on the page.
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<StructureSection load='3f4s' size='340' side='right'caption='[[3f4s]], [[Resolution|resolution]] 1.55&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'>[[3f4s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolbachia_endosymbiont_of_Drosophila_melanogaster Wolbachia endosymbiont of Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F4S FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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{{STRUCTURE_3f4s| PDB=3f4s | 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=3f4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f4s OCA], [https://pdbe.org/3f4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f4s RCSB], [https://www.ebi.ac.uk/pdbsum/3f4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f4s ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q73GA4_WOLPM Q73GA4_WOLPM]
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== Evolutionary Conservation ==
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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/f4/3f4s_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3f4s 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 ==
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The alpha-Proteobacterium Wolbachia pipientis is a highly successful intracellular endosymbiont of invertebrates that manipulates its host reproductive biology to facilitate its own maternal transmission. The fastidious nature of Wolbachia and the lack of genetic transformation have hampered analysis of the molecular basis of these manipulations. Structure determination of key Wolbachia proteins will enable development of inhibitors for chemical genetics studies. Wolbachia encodes a homolog (alpha-DsbA1) of the Escherichia coli dithiol oxidase enzyme EcDsbA essential for the oxidative folding of many exported proteins. We found that the active-site cysteine pair of Wolbachia alpha-DsbA1 has the most reducing redox potential of any characterised DsbA. In addition, Wolbachia alpha-DsbA1 possesses a second disulfide that is highly conserved in alpha-Proteobacterial DsbAs but not in other DsbAs. The alpha-DsbA1 structure lacks the characteristic hydrophobic features of EcDsbA and the protein neither complements EcDsbA deletion mutants in E. coli nor interacts with EcDsbB, the redox partner of EcDsbA. The surface characteristics and redox profile of alpha-DsbA1 indicate that it probably plays a specialised oxidative folding role with a narrow substrate specificity. This first report of a Wolbachia protein structure provides the basis for future chemical genetics studies.
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===Crystal structure of Wolbachia pipientis alpha-DsbA1 T172V===
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STRUCTURAL AND FUNCTIONAL CHARACTERISATION OF THE OXIDOREDUCTASE alpha-DSBA1 FROM WOLBACHIA PIPIENTIS.,Kurz M, Iturbe-Ormaetxe I, Jarrott R, Shouldice SR, Wouters MA, Frei P, Glockshuber R, Oneill S, Heras B, Martin J Antioxid Redox Signal. 2009 Mar 5. PMID:19265485<ref>PMID:19265485</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_19265485}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3f4s" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19265485 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19265485}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3F4S is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Wolbachia_endosymbiont_of_drosophila_melanogaster Wolbachia endosymbiont of drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F4S OCA].
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[[Category: Wolbachia endosymbiont of Drosophila melanogaster]]
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[[Category: Heras B]]
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==Reference==
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[[Category: Kurz M]]
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<ref group="xtra">PMID:19265485</ref><references group="xtra"/>
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[[Category: Martin JL]]
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[[Category: Wolbachia endosymbiont of drosophila melanogaster]]
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[[Category: Heras, B.]]
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[[Category: Kurz, M.]]
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[[Category: Martin, J L.]]
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[[Category: Dsba]]
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[[Category: Oxidoreductase]]
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[[Category: Thioredoxin-fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 10 18:53:06 2009''
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Current revision

Crystal structure of Wolbachia pipientis alpha-DsbA1 T172V

PDB ID 3f4s

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