5lzs
From Proteopedia
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(New page: '''Unreleased structure''' The entry 5lzs is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the mammalian ribosomal elongation complex with aminoacyl-tRNA, eEF1A, and didemnin B== | |
| + | <SX load='5lzs' size='340' side='right' viewer='molstar' caption='[[5lzs]], [[Resolution|resolution]] 3.31Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lzs]] 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=5LZS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LZS 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]] 3.31Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7C4:(2~{S})-~{N}-[(2~{R})-1-[[(3~{S},6~{S},8~{S},12~{S},13~{R},16~{S},17~{R},20~{S},23~{S})-13-[(2~{S})-BUTAN-2-YL]-20-[(4-METHOXYPHENYL)METHYL]-6,17,21-TRIMETHYL-3-(2-METHYLPROPYL)-12-OXIDANYL-2,5,7,10,15,19,22-HEPTAKIS(OXIDANYLIDENE)-8-PROPAN-2-YL-9,18-DIOXA-1,4,14,21-TETRAZABICYCLO[21.3.0]HEXACOSAN-16-YL]AMINO]-4-METHYL-1-OXIDANYLIDENE-PENTAN-2-YL]-~{N}-METHYL-1-[(2~{S})-2-OXIDANYLPROPANOYL]PYRROLIDINE-2-CARBOXAMIDE'>7C4</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=5lzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lzs OCA], [https://pdbe.org/5lzs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lzs RCSB], [https://www.ebi.ac.uk/pdbsum/5lzs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lzs ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RL8_RABIT RL8_RABIT] Component of the large ribosomal subunit (PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857).<ref>PMID:25601755</ref> <ref>PMID:26245381</ref> <ref>PMID:27863242</ref> <ref>PMID:30517857</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In eukaryotes, accurate protein synthesis relies on a family of translational GTPases that pair with specific decoding factors to decipher the mRNA code on ribosomes. We present structures of the mammalian ribosome engaged with decoding factorGTPase complexes representing intermediates of translation elongation (aminoacyl-tRNAeEF1A), termination (eRF1eRF3), and ribosome rescue (PelotaHbs1l). Comparative analyses reveal that each decoding factor exploits the plasticity of the ribosomal decoding center to differentially remodel ribosomal proteins and rRNA. This leads to varying degrees of large-scale ribosome movements and implies distinct mechanisms for communicating information from the decoding center to each GTPase. Additional structural snapshots of the translation termination pathway reveal the conformational changes that choreograph the accommodation of decoding factors into the peptidyl transferase center. Our results provide a structural framework for how different states of the mammalian ribosome are selectively recognized by the appropriate decoding factorGTPase complex to ensure translational fidelity. | ||
| - | + | Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes.,Shao S, Murray J, Brown A, Taunton J, Ramakrishnan V, Hegde RS Cell. 2016 Nov 17;167(5):1229-1240.e15. doi: 10.1016/j.cell.2016.10.046. PMID:27863242<ref>PMID:27863242</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5lzs" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] | ||
| + | *[[3D sructureseceptor for activated protein kinase C 1|3D sructureseceptor for activated protein kinase C 1]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: Brown A]] | ||
| + | [[Category: Hegde RS]] | ||
| + | [[Category: Murray J]] | ||
| + | [[Category: Ramakrishnan V]] | ||
| + | [[Category: Shao S]] | ||
| + | [[Category: Taunton J]] | ||
Current revision
Structure of the mammalian ribosomal elongation complex with aminoacyl-tRNA, eEF1A, and didemnin B
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