1pn6: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1pn6.gif|left|200px]]<br /><applet load="1pn6" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1pn6" />
-'''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 />
-==Overview==
+==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.==
-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.
+<SX load='1pn6' size='340' side='right' viewer='molstar' caption='[[1pn6]], [[Resolution|resolution]] 10.80&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+</table>
+== Function ==
+[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.
+== 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/pn/1pn6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1pn6 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-PN6 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].
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
+__TOC__
-==Reference==
+</SX>
-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]
+[[Category: Large Structures]]
-[[Category: Single protein]]
 [[Category: Thermus thermophilus]]
-[[Category: Ehrenberg, M.]]
+[[Category: Ehrenberg M]]
-[[Category: Frank, J.]]
+[[Category: Frank J]]
-[[Category: Rawat, U.]]
+[[Category: Rawat U]]
-[[Category: Sengupta, J.]]
+[[Category: Sengupta J]]
-[[Category: Valle, M.]]
+[[Category: Valle M]]
-[[Category: Zavialov, A.]]
+[[Category: Zavialov A]]
-[[Category: cryo-em]]
-[[Category: e.coli 70s ribosome]]
-[[Category: elongation factor-g]]
-[[Category: fitting of crystal structure]]
-[[Category: post-termination complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:56:14 2007''