8oin: Difference between revisions

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'''Unreleased structure'''


The entry 8oin is ON HOLD
==55S mammalian mitochondrial ribosome with mtRF1 and P-site tRNA==
<StructureSection load='8oin' size='340' side='right'caption='[[8oin]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8oin]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OIN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1MA:6-HYDRO-1-METHYLADENOSINE-5-MONOPHOSPHATE'>1MA</scene>, <scene name='pdbligand=5F0:(3~{S})-3-azanyl-4-methoxy-4-oxidanylidene-butanoic+acid'>5F0</scene>, <scene name='pdbligand=5MC:5-METHYLCYTIDINE-5-MONOPHOSPHATE'>5MC</scene>, <scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=AYA:N-ACETYLALANINE'>AYA</scene>, <scene name='pdbligand=B8T:4-methyl,+cytidine-5-monophosphate'>B8T</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MA6:6N-DIMETHYLADENOSINE-5-MONOPHOSHATE'>MA6</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MIA:2-METHYLTHIO-N6-ISOPENTENYL-ADENOSINE-5-MONOPHOSPHATE'>MIA</scene>, <scene name='pdbligand=OMG:O2-METHYLGUANOSINE-5-MONOPHOSPHATE'>OMG</scene>, <scene name='pdbligand=OMU:O2-METHYLURIDINE+5-MONOPHOSPHATE'>OMU</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=SAC:N-ACETYL-SERINE'>SAC</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</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=8oin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8oin OCA], [https://pdbe.org/8oin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8oin RCSB], [https://www.ebi.ac.uk/pdbsum/8oin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8oin ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F1STE5_PIG F1STE5_PIG]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The genetic code that specifies the identity of amino acids incorporated into proteins during protein synthesis is almost universally conserved. Mitochondrial genomes feature deviations from the standard genetic code, including the reassignment of two arginine codons to stop codons. The protein required for translation termination at these noncanonical stop codons to release the newly synthesized polypeptides is not currently known. In this study, we used gene editing and ribosomal profiling in combination with cryo-electron microscopy to establish that mitochondrial release factor 1 (mtRF1) detects noncanonical stop codons in human mitochondria by a previously unknown mechanism of codon recognition. We discovered that binding of mtRF1 to the decoding center of the ribosome stabilizes a highly unusual conformation in the messenger RNA in which the ribosomal RNA participates in specific recognition of the noncanonical stop codons.


Authors:  
Molecular basis of translation termination at noncanonical stop codons in human mitochondria.,Saurer M, Leibundgut M, Nadimpalli HP, Scaiola A, Schonhut T, Lee RG, Siira SJ, Rackham O, Dreos R, Lenarcic T, Kummer E, Gatfield D, Filipovska A, Ban N Science. 2023 May 5;380(6644):531-536. doi: 10.1126/science.adf9890. Epub 2023 , May 4. PMID:37141370<ref>PMID:37141370</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8oin" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Ban N]]
[[Category: Leibundgut M]]
[[Category: Saurer M]]
[[Category: Scaiola A]]
[[Category: Schoenhut T]]

Revision as of 11:21, 14 June 2023

55S mammalian mitochondrial ribosome with mtRF1 and P-site tRNA55S mammalian mitochondrial ribosome with mtRF1 and P-site tRNA

Structural highlights

8oin is a 10 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , , , , , , , , , , , , , , , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

F1STE5_PIG

Publication Abstract from PubMed

The genetic code that specifies the identity of amino acids incorporated into proteins during protein synthesis is almost universally conserved. Mitochondrial genomes feature deviations from the standard genetic code, including the reassignment of two arginine codons to stop codons. The protein required for translation termination at these noncanonical stop codons to release the newly synthesized polypeptides is not currently known. In this study, we used gene editing and ribosomal profiling in combination with cryo-electron microscopy to establish that mitochondrial release factor 1 (mtRF1) detects noncanonical stop codons in human mitochondria by a previously unknown mechanism of codon recognition. We discovered that binding of mtRF1 to the decoding center of the ribosome stabilizes a highly unusual conformation in the messenger RNA in which the ribosomal RNA participates in specific recognition of the noncanonical stop codons.

Molecular basis of translation termination at noncanonical stop codons in human mitochondria.,Saurer M, Leibundgut M, Nadimpalli HP, Scaiola A, Schonhut T, Lee RG, Siira SJ, Rackham O, Dreos R, Lenarcic T, Kummer E, Gatfield D, Filipovska A, Ban N Science. 2023 May 5;380(6644):531-536. doi: 10.1126/science.adf9890. Epub 2023 , May 4. PMID:37141370[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Saurer M, Leibundgut M, Nadimpalli HP, Scaiola A, Schönhut T, Lee RG, Siira SJ, Rackham O, Dreos R, Lenarčič T, Kummer E, Gatfield D, Filipovska A, Ban N. Molecular basis of translation termination at noncanonical stop codons in human mitochondria. Science. 2023 May 5;380(6644):531-536. PMID:37141370 doi:10.1126/science.adf9890

8oin, resolution 3.60Å

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