7a5h: Difference between revisions

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==Structure of the split human mitoribosomal large subunit with rescue factors mtRF-R and MTRES1==
<StructureSection load='7a5h' size='340' side='right'caption='[[7a5h]]' scene=''>
<StructureSection load='7a5h' size='340' side='right'caption='[[7a5h]], [[Resolution|resolution]] 3.30&Aring;' 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 [http://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
<table><tr><td colspan='2'>[[7a5h]] 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=7A5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A5H FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7a5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a5h OCA], [http://pdbe.org/7a5h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7a5h RCSB], [http://www.ebi.ac.uk/pdbsum/7a5h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7a5h ProSAT]</span></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MEQ:N5-METHYLGLUTAMINE'>MEQ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</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=7a5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a5h OCA], [https://pdbe.org/7a5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a5h RCSB], [https://www.ebi.ac.uk/pdbsum/7a5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a5h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RM02_HUMAN RM02_HUMAN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The human mitochondrial ribosome (mitoribosome) and associated proteins regulate the synthesis of 13 essential subunits of the oxidative phosphorylation complexes. We report the discovery of a mitoribosome-associated quality control pathway that responds to interruptions during elongation, and we present structures at 3.1- to 3.3-angstrom resolution of mitoribosomal large subunits trapped during ribosome rescue. Release factor homolog C12orf65 (mtRF-R) and RNA binding protein C6orf203 (MTRES1) eject the nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome biogenesis factors to these quality control intermediates suggests additional roles for these factors during mitoribosome rescue. We also report related cryo-electron microscopy structures (3.7 to 4.4 angstrom resolution) of elongating mitoribosomes bound to tRNAs, nascent polypeptides, the guanosine triphosphatase elongation factors mtEF-Tu and mtEF-G1, and the Oxa1L translocase.
Elongational stalling activates mitoribosome-associated quality control.,Desai N, Yang H, Chandrasekaran V, Kazi R, Minczuk M, Ramakrishnan V Science. 2020 Nov 27;370(6520):1105-1110. doi: 10.1126/science.abc7782. PMID:33243891<ref>PMID:33243891</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7a5h" 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: Z-disk]]
[[Category: Chandrasekaran V]]
[[Category: Desai N]]
[[Category: Kazi R]]
[[Category: Minczuk M]]
[[Category: Ramakrishnan V]]
[[Category: Yang H]]

Latest revision as of 09:09, 2 March 2023

Structure of the split human mitoribosomal large subunit with rescue factors mtRF-R and MTRES1Structure of the split human mitoribosomal large subunit with rescue factors mtRF-R and MTRES1

Structural highlights

7a5h is a 10 chain structure with sequence from Homo sapiens. 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

RM02_HUMAN

Publication Abstract from PubMed

The human mitochondrial ribosome (mitoribosome) and associated proteins regulate the synthesis of 13 essential subunits of the oxidative phosphorylation complexes. We report the discovery of a mitoribosome-associated quality control pathway that responds to interruptions during elongation, and we present structures at 3.1- to 3.3-angstrom resolution of mitoribosomal large subunits trapped during ribosome rescue. Release factor homolog C12orf65 (mtRF-R) and RNA binding protein C6orf203 (MTRES1) eject the nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome biogenesis factors to these quality control intermediates suggests additional roles for these factors during mitoribosome rescue. We also report related cryo-electron microscopy structures (3.7 to 4.4 angstrom resolution) of elongating mitoribosomes bound to tRNAs, nascent polypeptides, the guanosine triphosphatase elongation factors mtEF-Tu and mtEF-G1, and the Oxa1L translocase.

Elongational stalling activates mitoribosome-associated quality control.,Desai N, Yang H, Chandrasekaran V, Kazi R, Minczuk M, Ramakrishnan V Science. 2020 Nov 27;370(6520):1105-1110. doi: 10.1126/science.abc7782. PMID:33243891[1]

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

See Also

References

  1. Desai N, Yang H, Chandrasekaran V, Kazi R, Minczuk M, Ramakrishnan V. Elongational stalling activates mitoribosome-associated quality control. Science. 2020 Nov 27;370(6520):1105-1110. doi: 10.1126/science.abc7782. PMID:33243891 doi:http://dx.doi.org/10.1126/science.abc7782

7a5h, resolution 3.30Å

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OCA