7l08: Difference between revisions
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==== | ==Cryo-EM structure of the human 55S mitoribosome-RRFmt complex.== | ||
<StructureSection load='7l08' size='340' side='right'caption='[[7l08]]' scene=''> | <StructureSection load='7l08' size='340' side='right'caption='[[7l08]], [[Resolution|resolution]] 3.49Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7l08]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7L08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L08 FirstGlance]. <br> | ||
</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=7l08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l08 OCA], [https://pdbe.org/7l08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l08 RCSB], [https://www.ebi.ac.uk/pdbsum/7l08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l08 ProSAT]</span></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]] 3.49Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7l08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l08 OCA], [https://pdbe.org/7l08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l08 RCSB], [https://www.ebi.ac.uk/pdbsum/7l08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l08 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ribosomes are recycled for a new round of translation initiation by dissociation of ribosomal subunits, messenger RNA and transfer RNA from their translational post-termination complex. Here we present cryo-EM structures of the human 55S mitochondrial ribosome (mitoribosome) and the mitoribosomal large 39S subunit in complex with mitoribosome recycling factor (RRF(mt)) and a recycling-specific homolog of elongation factor G (EF-G2(mt)). These structures clarify an unusual role of a mitochondria-specific segment of RRF(mt), identify the structural distinctions that confer functional specificity to EF-G2(mt), and show that the deacylated tRNA remains with the dissociated 39S subunit, suggesting a distinct sequence of events in mitoribosome recycling. Furthermore, biochemical and structural analyses reveal that the molecular mechanism of antibiotic fusidic acid resistance for EF-G2(mt) is markedly different from that of mitochondrial elongation factor EF-G1(mt), suggesting that the two human EF-G(mt)s have evolved diversely to negate the effect of a bacterial antibiotic. | |||
Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance.,Koripella RK, Deep A, Agrawal EK, Keshavan P, Banavali NK, Agrawal RK Nat Commun. 2021 Jun 14;12(1):3607. doi: 10.1038/s41467-021-23726-4. PMID:34127662<ref>PMID:34127662</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7l08" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribosome 3D structures|Ribosome 3D structures]] | |||
*[[Ribosome recycling factor|Ribosome recycling factor]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Agrawal EK]] | ||
[[Category: Agrawal RK]] | |||
[[Category: Deep A]] | |||
[[Category: Koripella R]] | |||
Latest revision as of 11:56, 17 October 2024
Cryo-EM structure of the human 55S mitoribosome-RRFmt complex.Cryo-EM structure of the human 55S mitoribosome-RRFmt complex.
Structural highlights
Publication Abstract from PubMedRibosomes are recycled for a new round of translation initiation by dissociation of ribosomal subunits, messenger RNA and transfer RNA from their translational post-termination complex. Here we present cryo-EM structures of the human 55S mitochondrial ribosome (mitoribosome) and the mitoribosomal large 39S subunit in complex with mitoribosome recycling factor (RRF(mt)) and a recycling-specific homolog of elongation factor G (EF-G2(mt)). These structures clarify an unusual role of a mitochondria-specific segment of RRF(mt), identify the structural distinctions that confer functional specificity to EF-G2(mt), and show that the deacylated tRNA remains with the dissociated 39S subunit, suggesting a distinct sequence of events in mitoribosome recycling. Furthermore, biochemical and structural analyses reveal that the molecular mechanism of antibiotic fusidic acid resistance for EF-G2(mt) is markedly different from that of mitochondrial elongation factor EF-G1(mt), suggesting that the two human EF-G(mt)s have evolved diversely to negate the effect of a bacterial antibiotic. Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance.,Koripella RK, Deep A, Agrawal EK, Keshavan P, Banavali NK, Agrawal RK Nat Commun. 2021 Jun 14;12(1):3607. doi: 10.1038/s41467-021-23726-4. PMID:34127662[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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