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1t1m

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Revision as of 20:58, 10 September 2015

Binding position of ribosome recycling factor (RRF) on the E. coli 70S ribosome

Structural highlights

1t1m is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1kc9, 1fjf, 1dd5, 1ek8, 1t1o
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[P84154_ECOLX] 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).[HAMAP-Rule:MF_00040]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

After the termination step of protein synthesis, a deacylated tRNA and mRNA remain associated with the ribosome. The ribosome-recycling factor (RRF), together with elongation factor G (EF-G), disassembles this posttermination complex into mRNA, tRNA, and the ribosome. We have obtained a three-dimensional cryo-electron microscopic map of a complex of the Escherichia coli 70S ribosome and RRF. We find that RRF interacts mainly with the segments of the large ribosomal subunit's (50S) rRNA helices that are involved in the formation of two central intersubunit bridges, B2a and B3. The binding of RRF induces considerable conformational changes in some of the functional domains of the ribosome. As compared to its binding position derived previously by hydroxyl radical probing study, we find that RRF binds further inside the intersubunit space of the ribosome such that the tip of its domain I is shifted (by approximately 13 A) toward protein L5 within the central protuberance of the 50S subunit, and domain II is oriented more toward the small ribosomal subunit (30S). Overlapping binding sites of RRF, EF-G, and the P-site tRNA suggest that the binding of EF-G would trigger the removal of deacylated tRNA from the P site by moving RRF toward the ribosomal E site, and subsequent removal of mRNA may be induced by a shift in the position of 16S rRNA helix 44, which harbors part of the mRNA.

Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome: functional implications.,Agrawal RK, Sharma MR, Kiel MC, Hirokawa G, Booth TM, Spahn CM, Grassucci RA, Kaji A, Frank J Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8900-5. Epub 2004 Jun 3. PMID:15178758^[1]

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

References

↑ Agrawal RK, Sharma MR, Kiel MC, Hirokawa G, Booth TM, Spahn CM, Grassucci RA, Kaji A, Frank J. Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome: functional implications. Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8900-5. Epub 2004 Jun 3. PMID:15178758 doi:http://dx.doi.org/10.1073/pnas.0401904101

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t1m"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[1t1m]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T1M FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kc9|1kc9]], [[1fjf|1fjf]], [[1dd5|1dd5]], [[1ek8|1ek8]], [[1t1o|1t1o]]</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=1t1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t1m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t1m RCSB], [http://www.ebi.ac.uk/pdbsum/1t1m PDBsum]</span></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=1t1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t1m OCA], [http://pdbe.org/1t1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t1m RCSB], [http://www.ebi.ac.uk/pdbsum/1t1m PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1t1m" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ribosome recycling factor|Ribosome recycling factor]]
 == References ==
 <references/>

1t1m

From Proteopedia

Revision as of 20:58, 10 September 2015

Binding position of ribosome recycling factor (RRF) on the E. coli 70S ribosome

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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