1ls2

From Proteopedia

(Difference between revisions)

Revision as of 10:15, 12 January 2022

Fitting of EF-Tu and tRNA in the Low Resolution Cryo-EM Map of an EF-Tu Ternary Complex (GDP and Kirromycin) Bound to E. coli 70S Ribosome

1ls2, resolution 16.80Å

Structural highlights

1ls2 is a 2 chain structure with sequence from Escherichia coli and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1efc, 1ttt, 1exm, 1lu3
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Valle M, Sengupta J, Swami NK, Grassucci RA, Burkhardt N, Nierhaus KH, Agrawal RK, Frank J. Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process. EMBO J. 2002 Jul 1;21(13):3557-67. PMID:12093756 doi:10.1093/emboj/cdf326

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ls2"

@@ Line 3: / Line 3: @@
 <SX load='1ls2' size='340' side='right' viewer='molstar' caption='[[1ls2]], [[Resolution|resolution]] 16.80&Aring;' scene=''>
 == 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://proteopedia.org/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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1efc|1efc]], [[1ttt|1ttt]], [[1exm|1exm]], [[1lu3|1lu3]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
 == Evolutionary Conservation ==

1ls2

From Proteopedia

Revision as of 10:15, 12 January 2022

Fitting of EF-Tu and tRNA in the Low Resolution Cryo-EM Map of an EF-Tu Ternary Complex (GDP and Kirromycin) Bound to E. coli 70S Ribosome

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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