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3j0d

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Revision as of 17:37, 10 April 2020

Models for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complex

3j0d, resolution 11.10Å

Structural highlights

3j0d is a 11 chain structure with sequence from Escherichia coli and Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RRF_THET8] Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another (By similarity). [RL11_ECOLI] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B] [RS12_ECOLI] With S4 and S5 plays an important role in translational accuracy.[HAMAP-Rule:MF_00403_B] Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit (By similarity).[HAMAP-Rule:MF_00403_B] Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit.[HAMAP-Rule:MF_00403_B]

Publication Abstract from PubMed

The ribosome-recycling factor (RRF) and elongation factor-G (EF-G) disassemble the 70S post-termination complex (PoTC) into mRNA, tRNA, and two ribosomal subunits. We have determined cryo-electron microscopic structures of the PoTC.RRF complex, with and without EF-G. We find that domain II of RRF initially interacts with universally conserved residues of the 23S rRNA helices 43 and 95, and protein L11 within the 50S ribosomal subunit. Upon EF-G binding, both RRF and tRNA are driven towards the tRNA-exit (E) site, with a large rotational movement of domain II of RRF towards the 30S ribosomal subunit. During this intermediate step of the recycling process, domain II of RRF and domain IV of EF-G adopt hitherto unknown conformations. Furthermore, binding of EF-G to the PoTC.RRF complex reverts the ribosome from ratcheted to unratcheted state. These results suggest that (i) the ribosomal intersubunit reorganizations upon RRF binding and subsequent EF-G binding could be instrumental in destabilizing the PoTC and (ii) the modes of action of EF-G during tRNA translocation and ribosome-recycling steps are markedly different.

Structural insights into initial and intermediate steps of the ribosome-recycling process.,Yokoyama T, Shaikh TR, Iwakura N, Kaji H, Kaji A, Agrawal RK EMBO J. 2012 Mar 2;31(7):1836-46. doi: 10.1038/emboj.2012.22. PMID:22388519^[1]

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

References

↑ Yokoyama T, Shaikh TR, Iwakura N, Kaji H, Kaji A, Agrawal RK. Structural insights into initial and intermediate steps of the ribosome-recycling process. EMBO J. 2012 Mar 2;31(7):1836-46. doi: 10.1038/emboj.2012.22. PMID:22388519 doi:10.1038/emboj.2012.22

1 Structural highlights
2 Function
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/3j0d"

@@ Line 3: / Line 3: @@
 <SX load='3j0d' size='340' side='right' viewer='molstar' caption='[[3j0d]], [[Resolution|resolution]] 11.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3j0d]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J0D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J0D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3j0d]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J0D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3J0D FirstGlance]. <br>
-</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=3j0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0d OCA], [http://pdbe.org/3j0d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j0d RCSB], [http://www.ebi.ac.uk/pdbsum/3j0d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j0d ProSAT]</span></td></tr>
+</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=3j0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j0d OCA], [http://pdbe.org/3j0d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j0d RCSB], [http://www.ebi.ac.uk/pdbsum/3j0d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j0d ProSAT]</span></td></tr>
 </table>
 == Function ==

3j0d

From Proteopedia

Revision as of 17:37, 10 April 2020

Models for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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