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1jqm

From Proteopedia

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(New page: 200px<br /><applet load="1jqm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jqm" /> '''Fitting of L11 protein and elongation factor...)
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[[Image:1jqm.gif|left|200px]]<br /><applet load="1jqm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jqm" />
 
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'''Fitting of L11 protein and elongation factor G (EF-G) in the cryo-em map of e. coli 70S ribosome bound with EF-G, GDP and fusidic acid'''<br />
 
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==Overview==
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==Fitting of L11 protein and elongation factor G (EF-G) in the cryo-em map of e. coli 70S ribosome bound with EF-G, GDP and fusidic acid==
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L11 protein is located at the base of the L7/L12 stalk of the 50 S subunit, of the Escherichia coli ribosome. Because of the flexible nature of the, region, recent X-ray crystallographic studies of the 50 S subunit failed, to locate the N-terminal domain of the protein. We have determined the, position of the complete L11 protein by comparing a three-dimensional, cryo-EM reconstruction of the 70 S ribosome, isolated from a mutant, lacking ribosomal protein L11, with the three-dimensional map of the, wild-type ribosome. Fitting of the X-ray coordinates of L11-23 S RNA, complex and EF-G into the cryo-EM maps combined with molecular modeling, reveals that, following EF-G-dependent GTP hydrolysis, domain V of EF-G, intrudes into the cleft between the 23 S ribosomal RNA and the N-terminal, domain of L11 (where the antibiotic thiostrepton binds), causing the, N-terminal domain to move and thereby inducing the formation of the, arc-like connection with the G' domain of EF-G. The results provide a new, insight into the mechanism of EF-G-dependent translocation.
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<SX load='1jqm' size='340' side='right' viewer='molstar' caption='[[1jqm]], [[Resolution|resolution]] 18.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jqm]] is a 2 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=1JQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JQM 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]] 18&#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=1jqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jqm OCA], [https://pdbe.org/1jqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jqm RCSB], [https://www.ebi.ac.uk/pdbsum/1jqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jqm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RL11_THEMA RL11_THEMA] This protein binds directly to 23S ribosomal RNA.
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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/jq/1jqm_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=1jqm 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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1JQM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JQM OCA].
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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*[[Ribosomal protein L11 3D structures|Ribosomal protein L11 3D structures]]
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==Reference==
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__TOC__
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Localization of L11 protein on the ribosome and elucidation of its involvement in EF-G-dependent translocation., Agrawal RK, Linde J, Sengupta J, Nierhaus KH, Frank J, J Mol Biol. 2001 Aug 24;311(4):777-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11518530 11518530]
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</SX>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Agrawal, R.K.]]
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[[Category: Agrawal RK]]
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[[Category: Frank, J.]]
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[[Category: Frank J]]
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[[Category: Linde, J.]]
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[[Category: Linde J]]
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[[Category: Nierhaus, K.H.]]
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[[Category: Nierhaus KH]]
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[[Category: Segupta, J.]]
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[[Category: Segupta J]]
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[[Category: 70s e.coli ribosome]]
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[[Category: cryo-em]]
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[[Category: ef-g]]
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[[Category: gdp state]]
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[[Category: l11]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:29:16 2007''
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Current revision

Fitting of L11 protein and elongation factor G (EF-G) in the cryo-em map of e. coli 70S ribosome bound with EF-G, GDP and fusidic acid

1jqm, resolution 18.00Å

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