1qzd

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<SX load='1qzd' size='340' side='right' viewer='molstar' caption='[[1qzd]], [[Resolution|resolution]] 10.00&Aring;' scene=''>
<SX load='1qzd' size='340' side='right' viewer='molstar' caption='[[1qzd]], [[Resolution|resolution]] 10.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1qzd]] is a 1 chain structure with 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=1QZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QZD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1qzd]] 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=1QZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QZD FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ob2|1ob2]], [[1qza|1qza]], [[1qzb|1qzb]], [[1qzc|1qzc]], [[1r2w|1r2w]], [[1r2x|1r2x]]</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]] 10&#8491;</td></tr>
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<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=1qzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzd OCA], [http://pdbe.org/1qzd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qzd RCSB], [http://www.ebi.ac.uk/pdbsum/1qzd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qzd ProSAT]</span></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=1qzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzd OCA], [https://pdbe.org/1qzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qzd RCSB], [https://www.ebi.ac.uk/pdbsum/1qzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qzd ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/EFTU2_ECOLI EFTU2_ECOLI] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118]
== 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=1qzd 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=1qzd ConSurf].
<div style="clear:both"></div>
<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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Aminoacyl-tRNAs (aa-tRNAs) are delivered to the ribosome as part of the ternary complex of aa-tRNA, elongation factor Tu (EF-Tu) and GTP. Here, we present a cryo-electron microscopy (cryo-EM) study, at a resolution of approximately 9 A, showing that during the incorporation of the aa-tRNA into the 70S ribosome of Escherichia coli, the flexibility of aa-tRNA allows the initial codon recognition and its accommodation into the ribosomal A site. In addition, a conformational change observed in the GTPase-associated center (GAC) of the ribosomal 50S subunit may provide the mechanism by which the ribosome promotes a relative movement of the aa-tRNA with respect to EF-Tu. This relative rearrangement seems to facilitate codon recognition by the incoming aa-tRNA, and to provide the codon-anticodon recognition-dependent signal for the GTPase activity of EF-Tu. From these new findings we propose a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome.
 
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Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy.,Valle M, Zavialov A, Li W, Stagg SM, Sengupta J, Nielsen RC, Nissen P, Harvey SC, Ehrenberg M, Frank J Nat Struct Biol. 2003 Nov;10(11):899-906. Epub 2003 Oct 19. PMID:14566331<ref>PMID:14566331</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 1qzd" 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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== References ==
 
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<references/>
 
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__TOC__
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ehrenberg, M]]
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[[Category: Ehrenberg M]]
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[[Category: Frank, J]]
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[[Category: Frank J]]
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[[Category: Harvey, S C]]
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[[Category: Harvey SC]]
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[[Category: Li, W]]
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[[Category: Li W]]
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[[Category: Nielsen, R C]]
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[[Category: Nielsen RC]]
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[[Category: Nissen, P]]
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[[Category: Nissen P]]
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[[Category: Sengupta, J]]
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[[Category: Sengupta J]]
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[[Category: Stagg, S M]]
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[[Category: Stagg SM]]
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[[Category: Valle, M]]
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[[Category: Valle M]]
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[[Category: Zavialov, A]]
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[[Category: Zavialov A]]
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[[Category: Biosynthetic protein]]
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[[Category: Elongation factor]]
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Current revision

EF-Tu.kirromycin coordinates fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome

1qzd, resolution 10.00Å

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