6zm6: Difference between revisions

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<StructureSection load='6zm6' size='340' side='right'caption='[[6zm6]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
<StructureSection load='6zm6' size='340' side='right'caption='[[6zm6]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[6zm6]] is a 15 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.59&#8491;</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]] 2.59&#8491;</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='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>
<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 ==
== Function ==
[https://www.uniprot.org/uniprot/RM03_HUMAN RM03_HUMAN]  
[https://www.uniprot.org/uniprot/RT30_HUMAN RT30_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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6zm6" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribosome 3D structures|Ribosome 3D structures]]
*[[Ribosome 3D structures|Ribosome 3D structures]]
== References ==
<references/>
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</StructureSection>
</StructureSection>
Retrieved from "https://proteopedia.org/6zm6"