1ls2: Difference between revisions

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<SX load='1ls2' size='340' side='right' viewer='molstar' caption='[[1ls2]], [[Resolution|resolution]] 16.80&Aring;' scene=''>
<SX load='1ls2' size='340' side='right' viewer='molstar' caption='[[1ls2]], [[Resolution|resolution]] 16.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ls2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LS2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LS2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ls2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LS2 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1efc|1efc]], [[1ttt|1ttt]], [[1exm|1exm]], [[1lu3|1lu3]]</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='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=1ls2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ls2 OCA], [http://pdbe.org/1ls2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ls2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ls2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ls2 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=1ls2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ls2 OCA], [https://pdbe.org/1ls2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ls2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ls2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ls2 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=1ls2 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=1ls2 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<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 1ls2" 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/>
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[[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: Cryo-em]]
[[Category: Ef-tu]]
[[Category: Ternary complex]]
[[Category: Translation-rna complex]]
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