1qzd: Difference between revisions

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[[Image:1qzd.gif|left|200px]]<br /><applet load="1qzd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qzd" />
'''EF-Tu.kirromycin coordinates fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome'''<br />


==Overview==
==EF-Tu.kirromycin coordinates fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome==
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.
<SX load='1qzd' size='340' side='right' viewer='molstar' caption='[[1qzd]], [[Resolution|resolution]] 10.00&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
== Function ==
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qz/1qzd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>


==About this Structure==
==See Also==
1QZD is a [http://en.wikipedia.org/wiki/Single_protein 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].
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 
__TOC__
==Reference==
</SX>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=14566331 14566331]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ehrenberg, M.]]
[[Category: Ehrenberg M]]
[[Category: Frank, J.]]
[[Category: Frank J]]
[[Category: Harvey, S C.]]
[[Category: Harvey SC]]
[[Category: Li, W.]]
[[Category: Li W]]
[[Category: Nielsen, R C.]]
[[Category: Nielsen RC]]
[[Category: Nissen, P.]]
[[Category: Nissen P]]
[[Category: Sengupta, J.]]
[[Category: Sengupta J]]
[[Category: Stagg, S M.]]
[[Category: Stagg SM]]
[[Category: Valle, M.]]
[[Category: Valle M]]
[[Category: Zavialov, A.]]
[[Category: Zavialov A]]
[[Category: biosynthetic protein]]
[[Category: elongation factor]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:21 2008''

Latest revision as of 08:19, 14 February 2024

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

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