4v6a: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4v6a]] 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=3huw 3huw], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3hux 3hux], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3huy 3huy] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3huz 3huz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V6A FirstGlance]. <br> | <table><tr><td colspan='2'>[[4v6a]] 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=3huw 3huw], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3hux 3hux], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3huy 3huy] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3huz 3huz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V6A 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]] 3.1Å</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=4v6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v6a OCA], [https://pdbe.org/4v6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v6a RCSB], [https://www.ebi.ac.uk/pdbsum/4v6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v6a 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=4v6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v6a OCA], [https://pdbe.org/4v6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v6a RCSB], [https://www.ebi.ac.uk/pdbsum/4v6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v6a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 21:04, 20 September 2023
Structure of EF-P bound to the 70S ribosome.Structure of EF-P bound to the 70S ribosome.
Structural highlights
FunctionRS16_THET8 Binds to the lower part of the body of the 30S subunit, where it stabilizes two of its domains.[HAMAP-Rule:MF_00385] Publication Abstract from PubMedElongation factor P (EF-P) is an essential protein that stimulates the formation of the first peptide bond in protein synthesis. Here we report the crystal structure of EF-P bound to the Thermus thermophilus 70S ribosome along with the initiator transfer RNA N-formyl-methionyl-tRNA(i) (fMet-tRNA(i)(fMet)) and a short piece of messenger RNA (mRNA) at a resolution of 3.5 angstroms. EF-P binds to a site located between the binding site for the peptidyl tRNA (P site) and the exiting tRNA (E site). It spans both ribosomal subunits with its amino-terminal domain positioned adjacent to the aminoacyl acceptor stem and its carboxyl-terminal domain positioned next to the anticodon stem-loop of the P site-bound initiator tRNA. Domain II of EF-P interacts with the ribosomal protein L1, which results in the largest movement of the L1 stalk that has been observed in the absence of ratcheting of the ribosomal subunits. EF-P facilitates the proper positioning of the fMet-tRNA(i)(fMet) for the formation of the first peptide bond during translation initiation. Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome.,Blaha G, Stanley RE, Steitz TA Science. 2009 Aug 21;325(5943):966-70. PMID:19696344[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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