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==== | ==Human mitochondrial ribosome in complex with mRNA, A/A tRNA and P/P tRNA== | ||
<StructureSection load='6zm6' size='340' side='right'caption='[[6zm6]]' scene=''> | <StructureSection load='6zm6' size='340' side='right'caption='[[6zm6]], [[Resolution|resolution]] 2.59Å' 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'>[[6zm6]] 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=6ZM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZM6 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=6zm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zm6 OCA], [https://pdbe.org/6zm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zm6 RCSB], [https://www.ebi.ac.uk/pdbsum/6zm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zm6 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]] 2.59Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=AYA:N-ACETYLALANINE'>AYA</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=IAS:BETA-L-ASPARTIC+ACID'>IAS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene>, <scene name='pdbligand=THC:N-METHYLCARBONYLTHREONINE'>THC</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=6zm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zm6 OCA], [https://pdbe.org/6zm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zm6 RCSB], [https://www.ebi.ac.uk/pdbsum/6zm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zm6 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Disease == | |||
[https://www.uniprot.org/uniprot/RM03_HUMAN RM03_HUMAN] Combined oxidative phosphorylation defect type 9. The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RM03_HUMAN RM03_HUMAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mitochondrial ribosomes (mitoribosomes) are tethered to the mitochondrial inner membrane to facilitate the cotranslational membrane insertion of the synthesized proteins. We report cryo-electron microscopy structures of human mitoribosomes with nascent polypeptide, bound to the insertase oxidase assembly 1-like (OXA1L) through three distinct contact sites. OXA1L binding is correlated with a series of conformational changes in the mitoribosomal large subunit that catalyze the delivery of newly synthesized polypeptides. The mechanism relies on the folding of mL45 inside the exit tunnel, forming two specific constriction sites that would limit helix formation of the nascent chain. A gap is formed between the exit and the membrane, making the newly synthesized proteins accessible. Our data elucidate the basis by which mitoribosomes interact with the OXA1L insertase to couple protein synthesis and membrane delivery. | |||
Mechanism of membrane-tethered mitochondrial protein synthesis.,Itoh Y, Andrell J, Choi A, Richter U, Maiti P, Best RB, Barrientos A, Battersby BJ, Amunts A Science. 2021 Feb 19;371(6531):846-849. doi: 10.1126/science.abe0763. PMID:33602856<ref>PMID:33602856</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6zm6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribosome 3D structures|Ribosome 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Amunts A]] | ||
[[Category: Andrell J]] | |||
[[Category: Itoh Y]] | |||
Latest revision as of 13:54, 15 November 2023
Human mitochondrial ribosome in complex with mRNA, A/A tRNA and P/P tRNAHuman mitochondrial ribosome in complex with mRNA, A/A tRNA and P/P tRNA
Structural highlights
DiseaseRM03_HUMAN Combined oxidative phosphorylation defect type 9. The disease is caused by mutations affecting the gene represented in this entry. FunctionPublication Abstract from PubMedMitochondrial ribosomes (mitoribosomes) are tethered to the mitochondrial inner membrane to facilitate the cotranslational membrane insertion of the synthesized proteins. We report cryo-electron microscopy structures of human mitoribosomes with nascent polypeptide, bound to the insertase oxidase assembly 1-like (OXA1L) through three distinct contact sites. OXA1L binding is correlated with a series of conformational changes in the mitoribosomal large subunit that catalyze the delivery of newly synthesized polypeptides. The mechanism relies on the folding of mL45 inside the exit tunnel, forming two specific constriction sites that would limit helix formation of the nascent chain. A gap is formed between the exit and the membrane, making the newly synthesized proteins accessible. Our data elucidate the basis by which mitoribosomes interact with the OXA1L insertase to couple protein synthesis and membrane delivery. Mechanism of membrane-tethered mitochondrial protein synthesis.,Itoh Y, Andrell J, Choi A, Richter U, Maiti P, Best RB, Barrientos A, Battersby BJ, Amunts A Science. 2021 Feb 19;371(6531):846-849. doi: 10.1126/science.abe0763. PMID:33602856[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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