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1mvr: Difference between revisions

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<SX load='1mvr' size='340' side='right' viewer='molstar' caption='[[1mvr]], [[Resolution|resolution]] 12.80&Aring;' scene=''>
<SX load='1mvr' size='340' side='right' viewer='molstar' caption='[[1mvr]], [[Resolution|resolution]] 12.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mvr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MVR FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mvr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MVR FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gix|1gix]], [[1giy|1giy]], [[1mi6|1mi6]], [[1gqe|1gqe]]</div></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]] 12.8&#8491;</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=1mvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvr OCA], [https://pdbe.org/1mvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mvr RCSB], [https://www.ebi.ac.uk/pdbsum/1mvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvr 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=1mvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvr OCA], [https://pdbe.org/1mvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mvr RCSB], [https://www.ebi.ac.uk/pdbsum/1mvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mvr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RS12_THET8 RS12_THET8]] With S4 and S5 plays an important role in translational accuracy (By similarity).[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.[HAMAP-Rule:MF_00403_B] [[https://www.uniprot.org/uniprot/RL11_THEMA RL11_THEMA]] This protein binds directly to 23S ribosomal RNA.
[https://www.uniprot.org/uniprot/RS12_THET8 RS12_THET8] With S4 and S5 plays an important role in translational accuracy (By similarity).[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.[HAMAP-Rule:MF_00403_B]
== 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=1mvr 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=1mvr ConSurf].
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== Publication Abstract from PubMed ==
Protein synthesis takes place on the ribosome, where genetic information carried by messenger RNA is translated into a sequence of amino acids. This process is terminated when a stop codon moves into the ribosomal decoding centre (DC) and is recognized by a class-1 release factor (RF). RFs have a conserved GGQ amino-acid motif, which is crucial for peptide release and is believed to interact directly with the peptidyl-transferase centre (PTC) of the 50S ribosomal subunit. Another conserved motif of RFs (SPF in RF2) has been proposed to interact directly with stop codons in the DC of the 30S subunit. The distance between the DC and PTC is approximately 73 A. However, in the X-ray structure of RF2, SPF and GGQ are only 23 A apart, indicating that they cannot be at DC and PTC simultaneously. Here we show that RF2 is in an open conformation when bound to the ribosome, allowing GGQ to reach the PTC while still allowing SPF-stop-codon interaction. The results indicate new interpretations of accuracy in termination, and have implications for how the presence of a stop codon in the DC is signalled to PTC.
A cryo-electron microscopic study of ribosome-bound termination factor RF2.,Rawat UB, Zavialov AV, Sengupta J, Valle M, Grassucci RA, Linde J, Vestergaard B, Ehrenberg M, Frank J Nature. 2003 Jan 2;421(6918):87-90. PMID:12511960<ref>PMID:12511960</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mvr" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribosomal protein L11|Ribosomal protein L11]]
*[[Ribosomal protein L11 3D structures|Ribosomal protein L11 3D structures]]
*[[Ribosomal protein S12|Ribosomal protein S12]]
*[[Ribosomal protein S12|Ribosomal protein S12]]
== References ==
<references/>
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__TOC__
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[[Category: Escherichia coli]]
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ehrenberg, M]]
[[Category: Ehrenberg M]]
[[Category: Frank, J]]
[[Category: Frank J]]
[[Category: Grassucci, R A]]
[[Category: Grassucci RA]]
[[Category: Linde, J]]
[[Category: Linde J]]
[[Category: Rawat, U B]]
[[Category: Rawat UB]]
[[Category: Sengupta, J]]
[[Category: Sengupta J]]
[[Category: Valle, M]]
[[Category: Valle M]]
[[Category: Vestergaard, B]]
[[Category: Vestergaard B]]
[[Category: Zavialov, A V]]
[[Category: Zavialov AV]]
[[Category: Conformational change]]
[[Category: Release complex]]
[[Category: Rf2]]
[[Category: Ribosome]]

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