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1qzd
From Proteopedia
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<SX load='1qzd' size='340' side='right' viewer='molstar' caption='[[1qzd]], [[Resolution|resolution]] 10.00Å' scene=''> | <SX load='1qzd' size='340' side='right' viewer='molstar' caption='[[1qzd]], [[Resolution|resolution]] 10.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1qzd]] is a 1 chain structure with sequence from [ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 10Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> | ||
| + | == 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 == | == 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> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | |||
| - | 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> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <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]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Ehrenberg | + | [[Category: Ehrenberg M]] |
| - | [[Category: Frank | + | [[Category: Frank J]] |
| - | [[Category: Harvey | + | [[Category: Harvey SC]] |
| - | [[Category: Li | + | [[Category: Li W]] |
| - | [[Category: Nielsen | + | [[Category: Nielsen RC]] |
| - | [[Category: Nissen | + | [[Category: Nissen P]] |
| - | [[Category: Sengupta | + | [[Category: Sengupta J]] |
| - | [[Category: Stagg | + | [[Category: Stagg SM]] |
| - | [[Category: Valle | + | [[Category: Valle M]] |
| - | [[Category: Zavialov | + | [[Category: Zavialov A]] |
| - | + | ||
| - | + | ||
Current revision
EF-Tu.kirromycin coordinates fitted into the cryo-EM map of EF-Tu ternary complex (GDP.Kirromycin) bound 70S ribosome
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Categories: Escherichia coli | Large Structures | Ehrenberg M | Frank J | Harvey SC | Li W | Nielsen RC | Nissen P | Sengupta J | Stagg SM | Valle M | Zavialov A
