1jqm

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Current revision (07:41, 7 February 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<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>
<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eg0|1eg0]]</div></td></tr>
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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>
<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>
<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>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/RL11_THEMA RL11_THEMA]] This protein binds directly to 23S ribosomal RNA. [[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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[https://www.uniprot.org/uniprot/RL11_THEMA RL11_THEMA] This protein binds directly to 23S ribosomal RNA.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[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=1jqm ConSurf].
</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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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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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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:11518530<ref>PMID:11518530</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1jqm" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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*[[Ribosomal protein L11|Ribosomal protein L11]]
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*[[Ribosomal protein L11 3D structures|Ribosomal protein L11 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[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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[[Category: Ribosome]]
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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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