1ek8: Difference between revisions

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 <StructureSection load='1ek8' size='340' side='right'caption='[[1ek8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ek8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EK8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ek8]] is a 1 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=1EK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EK8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DEM:DECYLOXY-METHANOL'>DEM</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
+</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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ek8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ek8 OCA], [http://pdbe.org/1ek8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ek8 RCSB], [http://www.ebi.ac.uk/pdbsum/1ek8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ek8 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DEM:DECYLOXY-METHANOL'>DEM</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></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=1ek8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ek8 OCA], [https://pdbe.org/1ek8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ek8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ek8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ek8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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]
+[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]]
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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=1ek8 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-We have determined the crystal structure of the Escherichia coli ribosome recycling factor (RRF), which catalyzes the disassembly of the termination complex in protein synthesis. The L-shaped molecule consists of two domains: a triple-stranded antiparallel coiled-coil and an alpha/beta domain. The coil domain has a cylindrical shape and negatively charged surface, which are reminiscent of the anticodon arm of tRNA and domain IV of elongation factor EF-G. We suggest that RRF binds to the ribosomal A-site through its coil domain, which is a tRNA mimic. The relative position of the two domains is changed about an axis along the hydrophobic cleft in the hinge where the alkyl chain of a detergent molecule is bound. The tRNA mimicry and the domain movement observed in RRF provide a structural basis for understanding the role of RRF in protein synthesis.
-Crystal structure of the ribosome recycling factor from Escherichia coli.,Kim KK, Min K, Suh SW EMBO J. 2000 May 15;19(10):2362-70. PMID:10811627<ref>PMID:10811627</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1ek8" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Ribosome recycling factor|Ribosome recycling factor]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Kim, K K]]
+[[Category: Kim KK]]
-[[Category: Min, K]]
+[[Category: Min K]]
-[[Category: Suh, S W]]
+[[Category: Suh SW]]
-[[Category: Coiled coil]]
-[[Category: Ribosome]]
-[[Category: T-rna mimicry]]
-[[Category: Translation]]
-[[Category: Translation factor]]