1qzd

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[[Image:1qzd.gif|left|200px]]
 
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{{Structure
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==EF-Tu.kirromycin coordinates fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome==
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|PDB= 1qzd |SIZE=350|CAPTION= <scene name='initialview01'>1qzd</scene>
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<SX load='1qzd' size='340' side='right' viewer='molstar' caption='[[1qzd]], [[Resolution|resolution]] 10.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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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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|ACTIVITY=
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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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|GENE=
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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>
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}}
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</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]
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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/qz/1qzd_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=1qzd ConSurf].
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<div style="clear:both"></div>
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'''EF-Tu.kirromycin coordinates fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome'''
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==See Also==
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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__TOC__
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==Overview==
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</SX>
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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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==About this Structure==
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1QZD 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=1QZD OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14566331 14566331]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:44:48 2008''
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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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OCA

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