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| | <SX load='6sgc' size='340' side='right' viewer='molstar' caption='[[6sgc]], [[Resolution|resolution]] 2.80Å' scene=''> | | <SX load='6sgc' size='340' side='right' viewer='molstar' caption='[[6sgc]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6sgc]] is a 86 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SGC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sgc]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SGC FirstGlance]. <br> |
| - | </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=SPD:SPERMIDINE'>SPD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 2.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=12A:2-METHYLTHIO-N6-(AMINOCARBONYL-L-THREONYL)-ADENOSINE-5-MONOPHOSPHATE'>12A</scene>, <scene name='pdbligand=1MA:6-HYDRO-1-METHYLADENOSINE-5-MONOPHOSPHATE'>1MA</scene>, <scene name='pdbligand=2MU:2,5-DIMETHYLURIDINE-5-MONOPHOSPHATE'>2MU</scene>, <scene name='pdbligand=5MC:5-METHYLCYTIDINE-5-MONOPHOSPHATE'>5MC</scene>, <scene name='pdbligand=70U:5-(O-METHYLACETO)-2-THIO-2-DEOXY-URIDINE-5-MONOPHOSPHATE'>70U</scene>, <scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=H2U:5,6-DIHYDROURIDINE-5-MONOPHOSPHATE'>H2U</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12A:2-METHYLTHIO-N6-(AMINOCARBONYL-L-THREONYL)-ADENOSINE-5-MONOPHOSPHATE'>12A</scene>, <scene name='pdbligand=1MA:6-HYDRO-1-METHYLADENOSINE-5-MONOPHOSPHATE'>1MA</scene>, <scene name='pdbligand=2MU:2,5-DIMETHYLURIDINE-5-MONOPHOSPHATE'>2MU</scene>, <scene name='pdbligand=5MC:5-METHYLCYTIDINE-5-MONOPHOSPHATE'>5MC</scene>, <scene name='pdbligand=70U:5-(O-METHYLACETO)-2-THIO-2-DEOXY-URIDINE-5-MONOPHOSPHATE'>70U</scene>, <scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=H2U:5,6-DIHYDROURIDINE-5-MONOPHOSPHATE'>H2U</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</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=6sgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sgc OCA], [https://pdbe.org/6sgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sgc RCSB], [https://www.ebi.ac.uk/pdbsum/6sgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sgc 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=6sgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sgc OCA], [https://pdbe.org/6sgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sgc RCSB], [https://www.ebi.ac.uk/pdbsum/6sgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sgc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/U3KPD5_RABIT U3KPD5_RABIT]] Binds to the 23S rRNA.[RuleBase:RU000576] [[https://www.uniprot.org/uniprot/G1SS70_RABIT G1SS70_RABIT]] May play a role during erythropoiesis through regulation of transcription factor DDIT3.[HAMAP-Rule:MF_03122]
| + | [https://www.uniprot.org/uniprot/RL36_RABIT RL36_RABIT] Component of the large ribosomal subunit (PubMed:26245381, PubMed:27863242). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:26245381, PubMed:27863242).<ref>PMID:26245381</ref> <ref>PMID:27863242</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: European rabbit]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Brown, A]] | + | [[Category: Brown A]] |
| - | [[Category: Chandrasekaran, V]] | + | [[Category: Chandrasekaran V]] |
| - | [[Category: Choi, J]] | + | [[Category: Choi J]] |
| - | [[Category: Hegde, R S]] | + | [[Category: Hegde RS]] |
| - | [[Category: Juszkiewicz, S]] | + | [[Category: Juszkiewicz S]] |
| - | [[Category: Puglisi, J D]] | + | [[Category: Puglisi JD]] |
| - | [[Category: Ramakrishnan, V]] | + | [[Category: Ramakrishnan V]] |
| - | [[Category: Shao, S]] | + | [[Category: Shao S]] |
| - | [[Category: Polya tail]]
| + | |
| - | [[Category: Protein translation]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Ribosome stalling]]
| + | |
| Structural highlights
Function
RL36_RABIT Component of the large ribosomal subunit (PubMed:26245381, PubMed:27863242). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:26245381, PubMed:27863242).[1] [2]
Publication Abstract from PubMed
Faulty or damaged messenger RNAs are detected by the cell when translating ribosomes stall during elongation and trigger pathways of mRNA decay, nascent protein degradation and ribosome recycling. The most common mRNA defect in eukaryotes is probably inappropriate polyadenylation at near-cognate sites within the coding region. How ribosomes stall selectively when they encounter poly(A) is unclear. Here, we use biochemical and structural approaches in mammalian systems to show that poly-lysine, encoded by poly(A), favors a peptidyl-transfer RNA conformation suboptimal for peptide bond formation. This conformation partially slows elongation, permitting poly(A) mRNA in the ribosome's decoding center to adopt a ribosomal RNA-stabilized single-stranded helix. The reconfigured decoding center clashes with incoming aminoacyl-tRNA, thereby precluding elongation. Thus, coincidence detection of poly-lysine in the exit tunnel and poly(A) in the decoding center allows ribosomes to detect aberrant mRNAs selectively, stall elongation and trigger downstream quality control pathways essential for cellular homeostasis.
Mechanism of ribosome stalling during translation of a poly(A) tail.,Chandrasekaran V, Juszkiewicz S, Choi J, Puglisi JD, Brown A, Shao S, Ramakrishnan V, Hegde RS Nat Struct Mol Biol. 2019 Nov 25. pii: 10.1038/s41594-019-0331-x. doi:, 10.1038/s41594-019-0331-x. PMID:31768042[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Brown A, Shao S, Murray J, Hegde RS, Ramakrishnan V. Structural basis for stop codon recognition in eukaryotes. Nature. 2015 Aug 27;524(7566):493-6. doi: 10.1038/nature14896. Epub 2015 Aug 5. PMID:26245381 doi:http://dx.doi.org/10.1038/nature14896
- ↑ Shao S, Murray J, Brown A, Taunton J, Ramakrishnan V, Hegde RS. Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes. Cell. 2016 Nov 17;167(5):1229-1240.e15. doi: 10.1016/j.cell.2016.10.046. PMID:27863242 doi:http://dx.doi.org/10.1016/j.cell.2016.10.046
- ↑ Chandrasekaran V, Juszkiewicz S, Choi J, Puglisi JD, Brown A, Shao S, Ramakrishnan V, Hegde RS. Mechanism of ribosome stalling during translation of a poly(A) tail. Nat Struct Mol Biol. 2019 Nov 25. pii: 10.1038/s41594-019-0331-x. doi:, 10.1038/s41594-019-0331-x. PMID:31768042 doi:http://dx.doi.org/10.1038/s41594-019-0331-x
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