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1zn0

From Proteopedia

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Revision as of 07:10, 11 September 2015

Coordinates of RRF and EF-G fitted into Cryo-EM map of the 50S subunit bound with both EF-G (GDPNP) and RRF

Structural highlights

1zn0 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:	1pn6, 1ek8, 1p6g
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[RRF_ECOLI] 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.[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

Ribosome recycling, the disassembly of the posttermination complex after each round of protein synthesis, is an essential step in mRNA translation, but its mechanism has remained obscure. In eubacteria, recycling is catalyzed by RRF (ribosome recycling factor) and EF-G (elongation factor G). By using cryo-electron microscopy, we have obtained two density maps, one of the RRF bound posttermination complex and one of the 50S subunit bound with both EF-G and RRF. Comparing the two maps, we found domain I of RRF to be in the same orientation, while domain II in the EF-G-containing 50S subunit is extensively rotated (approximately 60 degrees) compared to its orientation in the 70S complex. Mapping the 50S conformation of RRF onto the 70S posttermination complex suggests that it can disrupt the intersubunit bridges B2a and B3, and thus effect a separation of the two subunits. These observations provide the structural basis for the mechanism by which the posttermination complex is split into subunits by the joint action of RRF and EF-G.

Mechanism for the disassembly of the posttermination complex inferred from cryo-EM studies.,Gao N, Zavialov AV, Li W, Sengupta J, Valle M, Gursky RP, Ehrenberg M, Frank J Mol Cell. 2005 Jun 10;18(6):663-74. PMID:15949441^[1]

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

References

↑ Gao N, Zavialov AV, Li W, Sengupta J, Valle M, Gursky RP, Ehrenberg M, Frank J. Mechanism for the disassembly of the posttermination complex inferred from cryo-EM studies. Mol Cell. 2005 Jun 10;18(6):663-74. PMID:15949441 doi:http://dx.doi.org/10.1016/j.molcel.2005.05.005

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/1zn0"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[1zn0]] 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=1ZN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZN0 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pn6|1pn6]], [[1ek8|1ek8]], [[1p6g|1p6g]]</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=1zn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zn0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1zn0 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=1zn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zn0 OCA], [http://pdbe.org/1zn0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1zn0 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 1zn0" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Elongation factor|Elongation factor]]
+*[[Ribosome recycling factor|Ribosome recycling factor]]
 == References ==
 <references/>

1zn0

From Proteopedia

Revision as of 07:10, 11 September 2015

Coordinates of RRF and EF-G fitted into Cryo-EM map of the 50S subunit bound with both EF-G (GDPNP) and RRF

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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