4v63: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4v63]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3d5a 3d5a], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3d5b 3d5b], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3d5c 3d5c] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3d5d 3d5d]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V63 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4v63]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3d5a 3d5a], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3d5b 3d5b], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3d5c 3d5c] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3d5d 3d5d]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V63 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]] 3.207Å</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=4v63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v63 OCA], [https://pdbe.org/4v63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v63 RCSB], [https://www.ebi.ac.uk/pdbsum/4v63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v63 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=4v63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v63 OCA], [https://pdbe.org/4v63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v63 RCSB], [https://www.ebi.ac.uk/pdbsum/4v63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v63 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 21:04, 20 September 2023
Structural basis for translation termination on the 70S ribosome.Structural basis for translation termination on the 70S ribosome.
Structural highlights
FunctionRS14Z_THET2 Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site (By similarity). Publication Abstract from PubMedAt termination of protein synthesis, type I release factors promote hydrolysis of the peptidyl-transfer RNA linkage in response to recognition of a stop codon. Here we describe the crystal structure of the Thermus thermophilus 70S ribosome in complex with the release factor RF1, tRNA and a messenger RNA containing a UAA stop codon, at 3.2 A resolution. The stop codon is recognized in a pocket formed by conserved elements of RF1, including its PxT recognition motif, and 16S ribosomal RNA. The codon and the 30S subunit A site undergo an induced fit that results in stabilization of a conformation of RF1 that promotes its interaction with the peptidyl transferase centre. Unexpectedly, the main-chain amide group of Gln 230 in the universally conserved GGQ motif of the factor is positioned to contribute directly to peptidyl-tRNA hydrolysis. Structural basis for translation termination on the 70S ribosome.,Laurberg M, Asahara H, Korostelev A, Zhu J, Trakhanov S, Noller HF Nature. 2008 Aug 14;454(7206):852-7. Epub 2008 Jul 2. PMID:18596689[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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