4bts: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4bts]] is a 40 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila] and [https://en.wikipedia.org/wiki/Tetrahymena_thermophila_SB210 Tetrahymena thermophila SB210]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bpe 4bpe], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bpn 4bpn], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bpo 4bpo] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bpp 4bpp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BTS FirstGlance]. <br> | <table><tr><td colspan='2'>[[4bts]] is a 40 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila] and [https://en.wikipedia.org/wiki/Tetrahymena_thermophila_SB210 Tetrahymena thermophila SB210]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bpe 4bpe], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bpn 4bpn], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bpo 4bpo] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4bpp 4bpp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BTS 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=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">X-ray diffraction, [[Resolution|Resolution]] 3.703Å</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=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=4bts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bts OCA], [https://pdbe.org/4bts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bts RCSB], [https://www.ebi.ac.uk/pdbsum/4bts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bts 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=4bts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bts OCA], [https://pdbe.org/4bts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bts RCSB], [https://www.ebi.ac.uk/pdbsum/4bts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bts ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/I7MK25_TETTS I7MK25_TETTS] Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity).[RuleBase:RU004365] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Eukaryotic translation initiation factors (eIFs) 1A and 1 are central players in the complex process of start-codon recognition. To improve mechanistic understanding of this process, we determined the crystal structure of the 40S ribosomal subunit in complex with eIF1A and eIF1 from Tetrahymena thermophila at a resolution of 3.7 A. It reveals the positions of the two factors on the 40S and the conformational changes that accompany their binding. | |||
The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A.,Weisser M, Voigts-Hoffmann F, Rabl J, Leibundgut M, Ban N Nat Struct Mol Biol. 2013 Jul 14. doi: 10.1038/nsmb.2622. PMID:23851459<ref>PMID:23851459</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4bts" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Ribosome 3D structures|Ribosome 3D structures]] | *[[Ribosome 3D structures|Ribosome 3D structures]] | ||
*[[3D sructureseceptor for activated protein kinase C 1|3D sructureseceptor for activated protein kinase C 1]] | *[[3D sructureseceptor for activated protein kinase C 1|3D sructureseceptor for activated protein kinase C 1]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 14:57, 20 December 2023
THE CRYSTAL STRUCTURE OF THE EUKARYOTIC 40S RIBOSOMAL SUBUNIT IN COMPLEX WITH EIF1 AND EIF1ATHE CRYSTAL STRUCTURE OF THE EUKARYOTIC 40S RIBOSOMAL SUBUNIT IN COMPLEX WITH EIF1 AND EIF1A
Structural highlights
FunctionI7MK25_TETTS Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity).[RuleBase:RU004365] Publication Abstract from PubMedEukaryotic translation initiation factors (eIFs) 1A and 1 are central players in the complex process of start-codon recognition. To improve mechanistic understanding of this process, we determined the crystal structure of the 40S ribosomal subunit in complex with eIF1A and eIF1 from Tetrahymena thermophila at a resolution of 3.7 A. It reveals the positions of the two factors on the 40S and the conformational changes that accompany their binding. The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A.,Weisser M, Voigts-Hoffmann F, Rabl J, Leibundgut M, Ban N Nat Struct Mol Biol. 2013 Jul 14. doi: 10.1038/nsmb.2622. PMID:23851459[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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