1pn6

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(New page: 200px<br /><applet load="1pn6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pn6" /> '''Domain-wise fitting of the crystal structure...)
Current revision (08:09, 14 February 2024) (edit) (undo)
 
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[[Image:1pn6.gif|left|200px]]<br /><applet load="1pn6" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1pn6" />
 
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'''Domain-wise fitting of the crystal structure of T.thermophilus EF-G into the low resolution map of the release complex.Puromycin.EFG.GDPNP of E.coli 70S ribosome.'''<br />
 
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==Overview==
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==Domain-wise fitting of the crystal structure of T.thermophilus EF-G into the low resolution map of the release complex.Puromycin.EFG.GDPNP of E.coli 70S ribosome.==
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During the ribosomal translocation, the binding of elongation factor G, (EF-G) to the pretranslocational ribosome leads to a ratchet-like rotation, of the 30S subunit relative to the 50S subunit in the direction of the, mRNA movement. By means of cryo-electron microscopy we observe that this, rotation is accompanied by a 20 A movement of the L1 stalk of the 50S, subunit, implying that this region is involved in the translocation of, deacylated tRNAs from the P to the E site. These ribosomal motions can, occur only when the P-site tRNA is deacylated. Prior to peptidyl-transfer, to the A-site tRNA or peptide removal, the presence of the charged P-site, tRNA locks the ribosome and prohibits both of these motions.
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<SX load='1pn6' size='340' side='right' viewer='molstar' caption='[[1pn6]], [[Resolution|resolution]] 10.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1pn6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PN6 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">Electron Microscopy, [[Resolution|Resolution]] 10.8&#8491;</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=1pn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pn6 OCA], [https://pdbe.org/1pn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pn6 RCSB], [https://www.ebi.ac.uk/pdbsum/1pn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pn6 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/EFG_THETH EFG_THETH] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
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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/pn/1pn6_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=1pn6 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1PN6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PN6 OCA].
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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__TOC__
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==Reference==
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</SX>
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Locking and unlocking of ribosomal motions., Valle M, Zavialov A, Sengupta J, Rawat U, Ehrenberg M, Frank J, Cell. 2003 Jul 11;114(1):123-34. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12859903 12859903]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Ehrenberg, M.]]
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[[Category: Ehrenberg M]]
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[[Category: Frank, J.]]
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[[Category: Frank J]]
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[[Category: Rawat, U.]]
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[[Category: Rawat U]]
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[[Category: Sengupta, J.]]
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[[Category: Sengupta J]]
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[[Category: Valle, M.]]
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[[Category: Valle M]]
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[[Category: Zavialov, A.]]
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[[Category: Zavialov A]]
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[[Category: cryo-em]]
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[[Category: e.coli 70s ribosome]]
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[[Category: elongation factor-g]]
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[[Category: fitting of crystal structure]]
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[[Category: post-termination complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:56:14 2007''
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Current revision

Domain-wise fitting of the crystal structure of T.thermophilus EF-G into the low resolution map of the release complex.Puromycin.EFG.GDPNP of E.coli 70S ribosome.

1pn6, resolution 10.80Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

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