1w26

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(New page: 200px<br /><applet load="1w26" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w26, resolution 2.70&Aring;" /> '''TRIGGER FACTOR IN CO...)
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[[Image:1w26.gif|left|200px]]<br /><applet load="1w26" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1w26, resolution 2.70&Aring;" />
 
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'''TRIGGER FACTOR IN COMPLEX WITH THE RIBOSOME FORMS A MOLECULAR CRADLE FOR NASCENT PROTEINS'''<br />
 
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==Overview==
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==Trigger Factor in Complex with the Ribosome forms a Molecular Cradle for Nascent Proteins==
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During protein biosynthesis, nascent polypeptide chains that emerge from, the ribosomal exit tunnel encounter ribosome-associated chaperones, which, assist their folding to the native state. Here we present a 2.7 A crystal, structure of Escherichia coli trigger factor, the best-characterized, chaperone of this type, together with the structure of its, ribosome-binding domain in complex with the Haloarcula marismortui large, ribosomal subunit. Trigger factor adopts a unique conformation resembling, a crouching dragon with separated domains forming the amino-terminal, ribosome-binding 'tail', the peptidyl-prolyl isomerase 'head', the, carboxy-terminal 'arms' and connecting regions building up the 'back'., From its attachment point on the ribosome, trigger factor projects the, extended domains over the exit of the ribosomal tunnel, creating a, protected folding space where nascent polypeptides may be shielded from, proteases and aggregation. This study sheds new light on our understanding, of co-translational protein folding, and suggests an unexpected mechanism, of action for ribosome-associated chaperones.
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<StructureSection load='1w26' size='340' side='right'caption='[[1w26]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1w26]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W26 FirstGlance]. <br>
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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]] 2.7&#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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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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=1w26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w26 OCA], [https://pdbe.org/1w26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w26 RCSB], [https://www.ebi.ac.uk/pdbsum/1w26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w26 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TIG_ECOLI TIG_ECOLI] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to nascent polypeptide chains via ribosomal protein L23 (PubMed:12226666). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity.<ref>PMID:8633085</ref> <ref>PMID:8521806</ref> <ref>PMID:14726952</ref>
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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/w2/1w26_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=1w26 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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During protein biosynthesis, nascent polypeptide chains that emerge from the ribosomal exit tunnel encounter ribosome-associated chaperones, which assist their folding to the native state. Here we present a 2.7 A crystal structure of Escherichia coli trigger factor, the best-characterized chaperone of this type, together with the structure of its ribosome-binding domain in complex with the Haloarcula marismortui large ribosomal subunit. Trigger factor adopts a unique conformation resembling a crouching dragon with separated domains forming the amino-terminal ribosome-binding 'tail', the peptidyl-prolyl isomerase 'head', the carboxy-terminal 'arms' and connecting regions building up the 'back'. From its attachment point on the ribosome, trigger factor projects the extended domains over the exit of the ribosomal tunnel, creating a protected folding space where nascent polypeptides may be shielded from proteases and aggregation. This study sheds new light on our understanding of co-translational protein folding, and suggests an unexpected mechanism of action for ribosome-associated chaperones.
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==About this Structure==
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Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins.,Ferbitz L, Maier T, Patzelt H, Bukau B, Deuerling E, Ban N Nature. 2004 Sep 30;431(7008):590-6. Epub 2004 Aug 29. PMID:15334087<ref>PMID:15334087</ref>
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1W26 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W26 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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Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins., Ferbitz L, Maier T, Patzelt H, Bukau B, Deuerling E, Ban N, Nature. 2004 Sep 30;431(7008):590-6. Epub 2004 Aug 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15334087 15334087]
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</div>
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<div class="pdbe-citations 1w26" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ban, N.]]
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[[Category: Ban N]]
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[[Category: Bukau, B.]]
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[[Category: Bukau B]]
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[[Category: Deuerling, E.]]
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[[Category: Deuerling E]]
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[[Category: Ferbitz, L.]]
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[[Category: Ferbitz L]]
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[[Category: Maier, T.]]
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[[Category: Maier T]]
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[[Category: Patzelt, H.]]
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[[Category: Patzelt H]]
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[[Category: cell division]]
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[[Category: chaperone]]
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[[Category: isomerase]]
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[[Category: nascent chain]]
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[[Category: protein folding]]
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[[Category: ribosome associated protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:12:12 2007''
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Current revision

Trigger Factor in Complex with the Ribosome forms a Molecular Cradle for Nascent Proteins

PDB ID 1w26

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