4v69
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4v69]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3fih 3fih] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3fik 3fik]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V69 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4v69]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3fih 3fih] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3fik 3fik]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V69 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.7Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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=4v69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v69 OCA], [https://pdbe.org/4v69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v69 RCSB], [https://www.ebi.ac.uk/pdbsum/4v69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v69 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=4v69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v69 OCA], [https://pdbe.org/4v69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v69 RCSB], [https://www.ebi.ac.uk/pdbsum/4v69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v69 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RS11_ECOLI RS11_ECOLI] Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome (By similarity).[HAMAP-Rule:MF_01310] | [https://www.uniprot.org/uniprot/RS11_ECOLI RS11_ECOLI] Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome (By similarity).[HAMAP-Rule:MF_01310] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | In translation, elongation factor Tu (EF-Tu) molecules deliver aminoacyl-tRNAs to the mRNA-programmed ribosome. The GTPase activity of EF-Tu is triggered by ribosome-induced conformational changes of the factor that play a pivotal role in the selection of the cognate aminoacyl-tRNAs. We present a 6.7-A cryo-electron microscopy map of the aminoacyl-tRNA x EF-Tu x GDP x kirromycin-bound Escherichia coli ribosome, together with an atomic model of the complex obtained through molecular dynamics flexible fitting. The model reveals the conformational changes in the conserved GTPase switch regions of EF-Tu that trigger hydrolysis of GTP, along with key interactions, including those between the sarcin-ricin loop and the P loop of EF-Tu, and between the effector loop of EF-Tu and a conserved region of the 16S rRNA. Our data suggest that GTP hydrolysis on EF-Tu is controlled through a hydrophobic gate mechanism. | ||
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| - | Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis.,Villa E, Sengupta J, Trabuco LG, LeBarron J, Baxter WT, Shaikh TR, Grassucci RA, Nissen P, Ehrenberg M, Schulten K, Frank J Proc Natl Acad Sci U S A. 2009 Jan 27;106(4):1063-8. Epub 2009 Jan 2. PMID:19122150<ref>PMID:19122150</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4v69" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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*[[Ribosome 3D structures|Ribosome 3D structures]] | *[[Ribosome 3D structures|Ribosome 3D structures]] | ||
*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]] | *[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
Current revision
Ternary complex-bound E.coli 70S ribosome.
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Categories: Escherichia coli | Large Structures | Baxter WT | Ehrenberg M | Frank J | Grassucci RA | LeBarron J | Nissen P | Schulten K | Sengupta J | Shaikh TR | Trabuco LG | Villa E
