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1oms

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(New page: 200px<br /><applet load="1oms" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oms, resolution 2.30&Aring;" /> '''Structure determinat...)
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[[Image:1oms.gif|left|200px]]<br /><applet load="1oms" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1oms, resolution 2.30&Aring;" />
 
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'''Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.'''<br />
 
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==Overview==
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==Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.==
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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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<StructureSection load='1oms' size='340' side='right'caption='[[1oms]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1oms]] is a 3 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=1OMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OMS FirstGlance]. <br>
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1OMS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4, PG4, SO2 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OMS OCA].
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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]] 2.3&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO2:SULFUR+DIOXIDE'>SO2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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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=1oms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oms OCA], [https://pdbe.org/1oms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oms RCSB], [https://www.ebi.ac.uk/pdbsum/1oms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oms ProSAT]</span></td></tr>
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Chaperone binding at the ribosomal exit tunnel., Kristensen O, Gajhede M, Structure. 2003 Dec;11(12):1547-56. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14656439 14656439]
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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/om/1oms_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=1oms ConSurf].
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<div style="clear:both"></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: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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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: GOL]]
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[[Category: PG4]]
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[[Category: SO2]]
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[[Category: SO4]]
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[[Category: alpha-beta structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:00:49 2007''
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Current revision

Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.

PDB ID 1oms

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