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6d6s

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==Solution structure of Trigger Factor dimer==
==Solution structure of Trigger Factor dimer==
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<StructureSection load='6d6s' size='340' side='right'caption='[[6d6s]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='6d6s' size='340' side='right'caption='[[6d6s]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6d6s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D6S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D6S FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6d6s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D6S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D6S FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tig, b0436, JW0426 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></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=6d6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d6s OCA], [https://pdbe.org/6d6s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d6s RCSB], [https://www.ebi.ac.uk/pdbsum/6d6s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d6s ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6d6s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d6s OCA], [http://pdbe.org/6d6s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d6s RCSB], [http://www.ebi.ac.uk/pdbsum/6d6s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d6s ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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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[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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Molecular chaperones alter the folding properties of cellular proteins via mechanisms that are not well understood. Here, we show that Trigger Factor (TF), an ATP-independent chaperone, exerts strikingly contrasting effects on the folding of non-native proteins as it transitions between a monomeric and a dimeric state. We used NMR spectroscopy to determine the atomic resolution structure of the 100 kDa dimeric TF. The structural data show that some of the substrate-binding sites are buried in the dimeric interface, explaining the lower affinity for protein substrates of the dimeric compared to the monomeric TF. Surprisingly, the dimeric TF associates faster with proteins and it exhibits stronger anti-aggregation and holdase activity than the monomeric TF. The structural data show that the dimer assembles in a way that substrate-binding sites in the two subunits form a large contiguous surface inside a cavity, thus accounting for the observed accelerated association with unfolded proteins. Our results demonstrate how the activity of a chaperone can be modulated to provide distinct functional outcomes in the cell.
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Oligomerization of a molecular chaperone modulates its activity.,Saio T, Kawagoe S, Ishimori K, Kalodimos CG Elife. 2018 May 1;7. pii: 35731. doi: 10.7554/eLife.35731. PMID:29714686<ref>PMID:29714686</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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<div class="pdbe-citations 6d6s" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Ishimori K]]
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[[Category: Ishimori, K]]
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[[Category: Kalodimos CG]]
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[[Category: Kalodimos, C G]]
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[[Category: Kawagoe S]]
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[[Category: Kawagoe, S]]
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[[Category: Saio T]]
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[[Category: Saio, T]]
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[[Category: Chaperone]]
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[[Category: Molecular chaperone]]
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[[Category: Oligomerization]]
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[[Category: Protein folding]]
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Current revision

Solution structure of Trigger Factor dimer

PDB ID 6d6s

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