1lu3: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1lu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LU3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1lu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LU3 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 16.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ls2|1ls2]], [[1efc|1efc]], [[1ttt|1ttt]], [[1exm|1exm]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene></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=1lu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lu3 OCA], [https://pdbe.org/1lu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1lu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lu3 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=1lu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lu3 OCA], [https://pdbe.org/1lu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lu3 RCSB], [https://www.ebi.ac.uk/pdbsum/1lu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lu3 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
During the elongation cycle of protein biosynthesis, the specific amino acid coded for by the mRNA is delivered by a complex that is comprised of the cognate aminoacyl-tRNA, elongation factor Tu and GTP. As this ternary complex binds to the ribosome, the anticodon end of the tRNA reaches the decoding center in the 30S subunit. Here we present the cryo- electron microscopy (EM) study of an Escherichia coli 70S ribosome-bound ternary complex stalled with an antibiotic, kirromycin. In the cryo-EM map the anticodon arm of the tRNA presents a new conformation that appears to facilitate the initial codon-anticodon interaction. Furthermore, the elbow region of the tRNA is seen to contact the GTPase-associated center on the 50S subunit of the ribosome, suggesting an active role of the tRNA in the transmission of the signal prompting the GTP hydrolysis upon codon recognition.
Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process.,Valle M, Sengupta J, Swami NK, Grassucci RA, Burkhardt N, Nierhaus KH, Agrawal RK, Frank J EMBO J. 2002 Jul 1;21(13):3557-67. PMID:12093756<ref>PMID:12093756</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1lu3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Agrawal, R K]]
[[Category: Agrawal RK]]
[[Category: Burkhardt, N]]
[[Category: Burkhardt N]]
[[Category: Frank, J]]
[[Category: Frank J]]
[[Category: Grassucci, R A]]
[[Category: Grassucci RA]]
[[Category: Nierhaus, K H]]
[[Category: Nierhaus KH]]
[[Category: Sengupta, J]]
[[Category: Sengupta J]]
[[Category: Swami, N K]]
[[Category: Swami NK]]
[[Category: Valle, M]]
[[Category: Valle M]]
[[Category: 70s e coli ribosome]]
[[Category: Conformational change]]
[[Category: Cryo-em]]
[[Category: Rna]]
[[Category: Ternary complex]]
[[Category: Trna]]

Latest revision as of 10:36, 14 February 2024

Separate Fitting of the Anticodon Loop Region of tRNA (nucleotide 26-42) in the Low Resolution Cryo-EM Map of an EF-Tu Ternary Complex (GDP and Kirromycin) Bound to E. coli 70S RibosomeSeparate Fitting of the Anticodon Loop Region of tRNA (nucleotide 26-42) in the Low Resolution Cryo-EM Map of an EF-Tu Ternary Complex (GDP and Kirromycin) Bound to E. coli 70S Ribosome

1lu3, resolution 16.80Å

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