4v5e: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4v5e]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wh1 2wh1], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wh2 2wh2], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wh3 2wh3], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wh4 2wh4], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jl5 2jl5], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jl6 2jl6], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jl7 2jl7] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jl8 2jl8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V5E FirstGlance]. <br> | <table><tr><td colspan='2'>[[4v5e]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wh1 2wh1], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wh2 2wh2], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wh3 2wh3], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wh4 2wh4], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jl5 2jl5], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jl6 2jl6], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jl7 2jl7] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jl8 2jl8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V5E 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]] 3.45Å</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=4v5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v5e OCA], [https://pdbe.org/4v5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v5e RCSB], [https://www.ebi.ac.uk/pdbsum/4v5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v5e 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=4v5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v5e OCA], [https://pdbe.org/4v5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v5e RCSB], [https://www.ebi.ac.uk/pdbsum/4v5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v5e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 13:40, 10 January 2024
Insights into translational termination from the structure of RF2 bound to the ribosomeInsights into translational termination from the structure of RF2 bound to the ribosome
Structural highlights
FunctionRS5_THET8 With S4 and S12 plays an important role in translational accuracy (By similarity).[HAMAP-Rule:MF_01307_B] Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Binds mRNA in the 70S ribosome, positioning it for translation.[HAMAP-Rule:MF_01307_B] Publication Abstract from PubMedThe termination of protein synthesis occurs through the specific recognition of a stop codon in the A site of the ribosome by a release factor (RF), which then catalyzes the hydrolysis of the nascent protein chain from the P-site transfer RNA. Here we present, at a resolution of 3.5 angstroms, the crystal structure of RF2 in complex with its cognate UGA stop codon in the 70S ribosome. The structure provides insight into how RF2 specifically recognizes the stop codon; it also suggests a model for the role of a universally conserved GGQ motif in the catalysis of peptide release. Insights into translational termination from the structure of RF2 bound to the ribosome.,Weixlbaumer A, Jin H, Neubauer C, Voorhees RM, Petry S, Kelley AC, Ramakrishnan V Science. 2008 Nov 7;322(5903):953-6. PMID:18988853[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
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