View source for 4v19


==Structure of the large subunit of the mammalian mitoribosome, part 1 of 2==
<SX load='4v19' size='340' side='right' viewer='molstar' caption='[[4v19]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4v19]] 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=4V19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V19 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]] 3.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4v19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v19 OCA], [https://pdbe.org/4v19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v19 RCSB], [https://www.ebi.ac.uk/pdbsum/4v19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v19 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F1RT79_PIG F1RT79_PIG] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mitochondrial ribosomes (mitoribosomes) are extensively modified ribosomes of bacterial descent specialized for the synthesis and insertion of membrane proteins that are critical for energy conversion and ATP production inside mitochondria. Mammalian mitoribosomes, which comprise 39S and 28S subunits, have diverged markedly from the bacterial ribosomes from which they are derived, rendering them unique compared to bacterial, eukaryotic cytosolic and fungal mitochondrial ribosomes. We have previously determined at 4.9 A resolution the architecture of the porcine (Sus scrofa) 39S subunit, which is highly homologous to the human mitoribosomal large subunit. Here we present the complete atomic structure of the porcine 39S large mitoribosomal subunit determined in the context of a stalled translating mitoribosome at 3.4 A resolution by cryo-electron microscopy and chemical crosslinking/mass spectrometry. The structure reveals the locations and the detailed folds of 50 mitoribosomal proteins, shows the highly conserved mitoribosomal peptidyl transferase active site in complex with its substrate transfer RNAs, and defines the path of the nascent chain in mammalian mitoribosomes along their idiosyncratic exit tunnel. Furthermore, we present evidence that a mitochondrial tRNA has become an integral component of the central protuberance of the 39S subunit where it architecturally substitutes for the absence of the 5S ribosomal RNA, a ubiquitous component of all cytoplasmic ribosomes.

The complete structure of the large subunit of the mammalian mitochondrial ribosome.,Greber BJ, Boehringer D, Leibundgut M, Bieri P, Leitner A, Schmitz N, Aebersold R, Ban N Nature. 2014 Oct 1. doi: 10.1038/nature13895. PMID:25271403<ref>PMID:25271403</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4v19" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ribosome 3D structures|Ribosome 3D structures]]
*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Aebersold R]]
[[Category: Ban N]]
[[Category: Bieri P]]
[[Category: Boehringer D]]
[[Category: Greber BJ]]
[[Category: Leibundgut M]]
[[Category: Leitner A]]
[[Category: Schmitz N]]