1p9y

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[[Image:1p9y.png|left|200px]]
 
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==Ribosome binding of E. coli Trigger Factor mutant F44L.==
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The line below this paragraph, containing "STRUCTURE_1p9y", creates the "Structure Box" on the page.
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<StructureSection load='1p9y' size='340' side='right'caption='[[1p9y]], [[Resolution|resolution]] 2.15&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'>[[1p9y]] 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=1P9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P9Y 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]] 2.15&#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=ACY:ACETIC+ACID'>ACY</scene></td></tr>
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{{STRUCTURE_1p9y| PDB=1p9y | 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=1p9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9y OCA], [https://pdbe.org/1p9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p9y RCSB], [https://www.ebi.ac.uk/pdbsum/1p9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p9y 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/p9/1p9y_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=1p9y 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 exit tunnel region of the ribosome is well established as a focal point for interaction between the components that guide the fate of nascent polypeptides. One of these, the chaperone trigger factor (TF), associates with the 50S ribosomal subunit through its N-terminal domain. Targeting of TF to ribosomes is crucial to achieve its remarkable efficiency in protein folding. A similar tight coupling to translation is found in signal recognition particle (SRP)-dependent protein translocation. Here, we report crystal structures of the E. coli TF ribosome binding domain. TF is structurally related to the Hsp33 chaperone but has a prominent ribosome anchor located as a tip of the molecule. This tip includes the previously established unique TF signature motif. Comparison reveals that this feature is not found in SRP structures. We identify a conserved helical kink as a hallmark of the TF structure that is most likely critical to ensure ribosome association.
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===Ribosome binding of E. coli Trigger Factor mutant F44L.===
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Chaperone binding at the ribosomal exit tunnel.,Kristensen O, Gajhede M Structure. 2003 Dec;11(12):1547-56. PMID:14656439<ref>PMID:14656439</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_14656439}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1p9y" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14656439 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14656439}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1p9y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9Y OCA].
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==Reference==
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<ref group="xtra">PMID:014656439</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Gajhede, M.]]
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[[Category: Gajhede M]]
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[[Category: Kristensen, O.]]
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[[Category: Kristensen O]]
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[[Category: Alpha-beta protein]]
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[[Category: Isomerase]]
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Current revision

Ribosome binding of E. coli Trigger Factor mutant F44L.

PDB ID 1p9y

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