View source for 2vrh


==Structure of the E. coli trigger factor bound to a translating ribosome==
<SX load='2vrh' size='340' side='right' viewer='molstar' caption='[[2vrh]], [[Resolution|resolution]] 19.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vrh]] is a 4 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=2VRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VRH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 19&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vrh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrh OCA], [https://pdbe.org/2vrh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vrh RCSB], [https://www.ebi.ac.uk/pdbsum/2vrh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrh ProSAT]</span></td></tr>
</table>
== Function ==
[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> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vr/2vrh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2vrh ConSurf].
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== Publication Abstract from PubMed ==
Ribosome-associated chaperone Trigger Factor (TF) initiates folding of newly synthesized proteins in bacteria. Here, we pinpoint by site-specific crosslinking the sequence of molecular interactions of Escherichia coli TF and nascent chains during translation. Furthermore, we provide the first full-length structure of TF associated with ribosome-nascent chain complexes by using cryo-electron microscopy. In its active state, TF arches over the ribosomal exit tunnel accepting nascent chains in a protective void. The growing nascent chain initially follows a predefined path through the entire interior of TF in an unfolded conformation, and even after folding into a domain it remains accommodated inside the protective cavity of ribosome-bound TF. The adaptability to accept nascent chains of different length and folding states may explain how TF is able to assist co-translational folding of all kinds of nascent polypeptides during ongoing synthesis. Moreover, we suggest a model of how TF's chaperoning function can be coordinated with the co-translational processing and membrane targeting of nascent polypeptides by other ribosome-associated factors.

Molecular mechanism and structure of Trigger Factor bound to the translating ribosome.,Merz F, Boehringer D, Schaffitzel C, Preissler S, Hoffmann A, Maier T, Rutkowska A, Lozza J, Ban N, Bukau B, Deuerling E EMBO J. 2008 Jun 4;27(11):1622-32. Epub 2008 May 22. PMID:18497744<ref>PMID:18497744</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2vrh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ribosomal protein L23|Ribosomal protein L23]]
*[[Ribosomal protein L24|Ribosomal protein L24]]
*[[Ribosomal protein L29|Ribosomal protein L29]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Ban N]]
[[Category: Boehringer D]]
[[Category: Bukau B]]
[[Category: Deuerling E]]
[[Category: Hoffmann A]]
[[Category: Lozza J]]
[[Category: Maier T]]
[[Category: Merz F]]
[[Category: Preissler S]]
[[Category: Rutkowska A]]
[[Category: Schaffitzel C]]