1zn0: Difference between revisions

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-[[Image:1zn0.gif|left|200px]]
-<!--
+==Coordinates of RRF and EF-G fitted into Cryo-EM map of the 50S subunit bound with both EF-G (GDPNP) and RRF==
-The line below this paragraph, containing "STRUCTURE_1zn0", creates the "Structure Box" on the page.
+<SX load='1zn0' size='340' side='right' viewer='molstar' caption='[[1zn0]], [[Resolution|resolution]] 15.50&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1zn0]] 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=1ZN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZN0 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 15.5&#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=1zn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zn0 OCA], [https://pdbe.org/1zn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zn0 RCSB], [https://www.ebi.ac.uk/pdbsum/1zn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zn0 ProSAT]</span></td></tr>
-{{STRUCTURE_1zn0|  PDB=1zn0  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RRF_ECOLI RRF_ECOLI] Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.[HAMAP-Rule:MF_00040]
+== 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/zn/1zn0_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=1zn0 ConSurf].
+<div style="clear:both"></div>
-'''Coordinates of RRF and EF-G fitted into Cryo-EM map of the 50S subunit bound with both EF-G (GDPNP) and RRF'''
+==See Also==
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
+*[[Ribosome 3D structures|Ribosome 3D structures]]
-==Overview==
+*[[Ribosome recycling factor|Ribosome recycling factor]]
-Ribosome recycling, the disassembly of the posttermination complex after each round of protein synthesis, is an essential step in mRNA translation, but its mechanism has remained obscure. In eubacteria, recycling is catalyzed by RRF (ribosome recycling factor) and EF-G (elongation factor G). By using cryo-electron microscopy, we have obtained two density maps, one of the RRF bound posttermination complex and one of the 50S subunit bound with both EF-G and RRF. Comparing the two maps, we found domain I of RRF to be in the same orientation, while domain II in the EF-G-containing 50S subunit is extensively rotated (approximately 60 degrees) compared to its orientation in the 70S complex. Mapping the 50S conformation of RRF onto the 70S posttermination complex suggests that it can disrupt the intersubunit bridges B2a and B3, and thus effect a separation of the two subunits. These observations provide the structural basis for the mechanism by which the posttermination complex is split into subunits by the joint action of RRF and EF-G.
+__TOC__
+</SX>
-==About this Structure==
-ZN0 is a [[Single protein]] structure of 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=1ZN0 OCA].
-==Reference==
-Mechanism for the disassembly of the posttermination complex inferred from cryo-EM studies., Gao N, Zavialov AV, Li W, Sengupta J, Valle M, Gursky RP, Ehrenberg M, Frank J, Mol Cell. 2005 Jun 10;18(6):663-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15949441 15949441]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Ehrenberg, M.]]
+[[Category: Ehrenberg M]]
-[[Category: Frank, J.]]
+[[Category: Frank J]]
-[[Category: Gao, N.]]
+[[Category: Gao N]]
-[[Category: Gursky, R P.]]
+[[Category: Gursky RP]]
-[[Category: Li, W.]]
+[[Category: Li W]]
-[[Category: Sengupta, J.]]
+[[Category: Sengupta J]]
-[[Category: Valle, M.]]
+[[Category: Valle M]]
-[[Category: Zavialov, A V.]]
+[[Category: Zavialov AV]]
-[[Category: 50s subunit]]
-[[Category: Elongation factor g]]
-[[Category: Ribosome recycling factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:49:41 2008''