1ge9: Difference between revisions
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== | ==SOLUTION STRUCTURE OF THE RIBOSOME RECYCLING FACTOR== | ||
<StructureSection load='1ge9' size='340' side='right'caption='[[1ge9]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ge9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GE9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1ge9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ge9 OCA], [https://pdbe.org/1ge9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ge9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ge9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ge9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RRF_AQUAE RRF_AQUAE] 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). | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ge/1ge9_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1ge9 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The solution structure of ribosome recycling factor (RRF) from hyperthermophilic bacterium, Aquifex aeolicus, was determined by heteronuclear multidimensional NMR spectroscopy. Fifteen structures were calculated using restraints derived from NOE, J-coupling, and T1/T2 anisotropies. The resulting structure has an overall L-shaped conformation with two domains and is similar to that of a tRNA molecule. The domain I (corresponding to the anticodon stem of tRNA) is a rigid three alpha-helix bundle. Being slightly different from usual coiled-coil arrangements, each helix of domain I is not twisted but straight and parallel to the main axis. The domain II (corresponding to the portion with the CCA end of tRNA) is an alpha/beta domain with an alpha-helix and two beta-sheets, that has some flexible regions. The backbone atomic root-mean-square deviation (rmsd) values of both domains were 0.7 A when calculated separately, which is smaller than that of the molecule as a whole (1.4 A). Measurement of 15N-[1H] NOE values show that the residues in the corner of the L-shaped molecule are undergoing fast internal motion. These results indicate that the joint region between two domains contributes to the fluctuation in the orientation of two domains. Thus, it was shown that RRF remains the tRNA mimicry in solution where it functions. | The solution structure of ribosome recycling factor (RRF) from hyperthermophilic bacterium, Aquifex aeolicus, was determined by heteronuclear multidimensional NMR spectroscopy. Fifteen structures were calculated using restraints derived from NOE, J-coupling, and T1/T2 anisotropies. The resulting structure has an overall L-shaped conformation with two domains and is similar to that of a tRNA molecule. The domain I (corresponding to the anticodon stem of tRNA) is a rigid three alpha-helix bundle. Being slightly different from usual coiled-coil arrangements, each helix of domain I is not twisted but straight and parallel to the main axis. The domain II (corresponding to the portion with the CCA end of tRNA) is an alpha/beta domain with an alpha-helix and two beta-sheets, that has some flexible regions. The backbone atomic root-mean-square deviation (rmsd) values of both domains were 0.7 A when calculated separately, which is smaller than that of the molecule as a whole (1.4 A). Measurement of 15N-[1H] NOE values show that the residues in the corner of the L-shaped molecule are undergoing fast internal motion. These results indicate that the joint region between two domains contributes to the fluctuation in the orientation of two domains. Thus, it was shown that RRF remains the tRNA mimicry in solution where it functions. | ||
Solution structure of the ribosome recycling factor from Aquifex aeolicus.,Yoshida T, Uchiyama S, Nakano H, Kashimori H, Kijima H, Ohshima T, Saihara Y, Ishino T, Shimahara H, Yoshida T, Yokose K, Ohkubo T, Kaji A, Kobayashi Y Biochemistry. 2001 Feb 27;40(8):2387-96. PMID:11327859<ref>PMID:11327859</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ge9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribosome recycling factor|Ribosome recycling factor]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Ishino | [[Category: Ishino T]] | ||
[[Category: Kaji | [[Category: Kaji A]] | ||
[[Category: Kashimori | [[Category: Kashimori H]] | ||
[[Category: Kijima | [[Category: Kijima H]] | ||
[[Category: Kobayashi | [[Category: Kobayashi Y]] | ||
[[Category: Nakano | [[Category: Nakano H]] | ||
[[Category: Ohkubo | [[Category: Ohkubo T]] | ||
[[Category: Ohshima | [[Category: Ohshima T]] | ||
[[Category: Saihara | [[Category: Saihara Y]] | ||
[[Category: Shimahara | [[Category: Shimahara T]] | ||
[[Category: Uchiyama | [[Category: Uchiyama S]] | ||
[[Category: Yokose | [[Category: Yokose K]] | ||
[[Category: Yoshida | [[Category: Yoshida T]] | ||
Latest revision as of 02:30, 28 December 2023
SOLUTION STRUCTURE OF THE RIBOSOME RECYCLING FACTORSOLUTION STRUCTURE OF THE RIBOSOME RECYCLING FACTOR
Structural highlights
FunctionRRF_AQUAE 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). 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 PubMedThe solution structure of ribosome recycling factor (RRF) from hyperthermophilic bacterium, Aquifex aeolicus, was determined by heteronuclear multidimensional NMR spectroscopy. Fifteen structures were calculated using restraints derived from NOE, J-coupling, and T1/T2 anisotropies. The resulting structure has an overall L-shaped conformation with two domains and is similar to that of a tRNA molecule. The domain I (corresponding to the anticodon stem of tRNA) is a rigid three alpha-helix bundle. Being slightly different from usual coiled-coil arrangements, each helix of domain I is not twisted but straight and parallel to the main axis. The domain II (corresponding to the portion with the CCA end of tRNA) is an alpha/beta domain with an alpha-helix and two beta-sheets, that has some flexible regions. The backbone atomic root-mean-square deviation (rmsd) values of both domains were 0.7 A when calculated separately, which is smaller than that of the molecule as a whole (1.4 A). Measurement of 15N-[1H] NOE values show that the residues in the corner of the L-shaped molecule are undergoing fast internal motion. These results indicate that the joint region between two domains contributes to the fluctuation in the orientation of two domains. Thus, it was shown that RRF remains the tRNA mimicry in solution where it functions. Solution structure of the ribosome recycling factor from Aquifex aeolicus.,Yoshida T, Uchiyama S, Nakano H, Kashimori H, Kijima H, Ohshima T, Saihara Y, Ishino T, Shimahara H, Yoshida T, Yokose K, Ohkubo T, Kaji A, Kobayashi Y Biochemistry. 2001 Feb 27;40(8):2387-96. PMID:11327859[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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