6vmi
From Proteopedia
(Difference between revisions)
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- | ==== | + | ==Structure of the human mitochondrial ribosome-EF-G1 complex (ClassIII)== |
- | <StructureSection load='6vmi' size='340' side='right'caption='[[6vmi]]' scene=''> | + | <StructureSection load='6vmi' size='340' side='right'caption='[[6vmi]], [[Resolution|resolution]] 2.96Å' 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'>[[6vmi]] is a 12 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=6VMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VMI 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=6vmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vmi OCA], [https://pdbe.org/6vmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vmi RCSB], [https://www.ebi.ac.uk/pdbsum/6vmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vmi 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]] 2.96Å</td></tr> |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P5P:PURINE+RIBOSIDE-5-MONOPHOSPHATE'>P5P</scene>, <scene name='pdbligand=Y5P:1-(5-O-PHOSPHONO-BETA-D-RIBOFURANOSYL)-1,4-DIHYDROPYRIMIDINE'>Y5P</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=6vmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vmi OCA], [https://pdbe.org/6vmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vmi RCSB], [https://www.ebi.ac.uk/pdbsum/6vmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vmi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/RT10_HUMAN RT10_HUMAN] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The mammalian mitochondrial ribosome (mitoribosome) and its associated translational factors have evolved to accommodate greater participation of proteins in mitochondrial translation. Here we present the 2.68-3.96 A cryo-EM structures of the human 55S mitoribosome in complex with the human mitochondrial elongation factor G1 (EF-G1(mt)) in three distinct conformational states, including an intermediate state and a post-translocational state. These structures reveal the role of several mitochondria-specific (mito-specific) mitoribosomal proteins (MRPs) and a mito-specific segment of EF-G1(mt) in mitochondrial tRNA (tRNA(mt)) translocation. In particular, the mito-specific C-terminal extension in EF-G1(mt) is directly involved in translocation of the acceptor arm of the A-site tRNA(mt). In addition to the ratchet-like and independent head-swiveling motions exhibited by the small mitoribosomal subunit, we discover significant conformational changes in MRP mL45 at the nascent polypeptide-exit site within the large mitoribosomal subunit that could be critical for tethering of the elongating mitoribosome onto the inner-mitochondrial membrane. | ||
+ | |||
+ | Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation.,Koripella RK, Sharma MR, Bhargava K, Datta PP, Kaushal PS, Keshavan P, Spremulli LL, Banavali NK, Agrawal RK Nat Commun. 2020 Jul 31;11(1):3830. doi: 10.1038/s41467-020-17715-2. PMID:32737313<ref>PMID:32737313</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6vmi" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Elongation factor 3D structures|Elongation factor 3D structures]] | ||
+ | *[[Ribosome 3D structures|Ribosome 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Agrawal RK]] |
+ | [[Category: Koripella RK]] | ||
+ | [[Category: Sharma MR]] |
Current revision
Structure of the human mitochondrial ribosome-EF-G1 complex (ClassIII)
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