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3izp

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==Conformation of EF-G during translocation==
==Conformation of EF-G during translocation==
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<StructureSection load='3izp' size='340' side='right' caption='[[3izp]]' scene=''>
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<SX load='3izp' size='340' side='right' viewer='molstar' caption='[[3izp]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3izp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IZP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IZP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3izp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IZP FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fnm|1fnm]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3izp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3izp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3izp RCSB], [http://www.ebi.ac.uk/pdbsum/3izp PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3izp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3izp OCA], [https://pdbe.org/3izp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3izp RCSB], [https://www.ebi.ac.uk/pdbsum/3izp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3izp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/EFG_THETH EFG_THETH]] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
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[https://www.uniprot.org/uniprot/EFG_THETH EFG_THETH] Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Elongation factor G (EF-G) plays a crucial role in two stages of mRNA-(tRNA)(2) translocation. First, EF-G*GTP enters the pre-translocational ribosome in its intersubunit-rotated state, with tRNAs in their hybrid (P/E and A/P) positions. Second, a conformational change in EF-G's Domain IV induced by GTP hydrolysis disengages the mRNA-anticodon stem-loops of the tRNAs from the decoding center to advance relative to the small subunit when the ribosome undergoes a backward inter-subunit rotation. These events take place as EF-G undergoes a series of large conformational changes as visualized by cryo-EM and X-ray studies. The number and variety of these structures leave open many questions on how these different configurations form during the dynamic translocation process. To understand the molecular mechanism of translocation, we examined the molecular motions of EF-G in solution by means of molecular dynamics simulations. Our results show: (1) rotations of the super-domain formed by Domains III-V with respect to the super-domain formed by I-II, and rotations of Domain IV with respect to Domain III; (2) flexible conformations of both 503- and 575-loops; (3) large conformational variability in the bound form caused by the interaction between Domain V and the GTPase-associated center; (4) after GTP hydrolysis, the Switch I region seems to be instrumental for effecting the conformational change at the end of Domain IV implicated in the disengagement of the codon-anticodon helix from the decoding center. Proteins 2011; (c) 2011 Wiley-Liss, Inc.
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Molecular dynamics of EF-G during translocation.,Li W, Trabuco LG, Schulten K, Frank J Proteins. 2011 Jan 4. doi: 10.1002/prot.22976. PMID:21365677<ref>PMID:21365677</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Elongation factor|Elongation factor]]
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Frank, J]]
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[[Category: Frank J]]
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[[Category: Li, W]]
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[[Category: Li W]]
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[[Category: Schulten, K]]
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[[Category: Schulten K]]
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[[Category: Trabuco, L G]]
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[[Category: Trabuco LG]]
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[[Category: Electron microscopy]]
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[[Category: Flexible fitting]]
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[[Category: Gtp hydrolysis]]
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[[Category: Hybrid state]]
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[[Category: Inter-subunit rotation]]
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[[Category: Ribosomal protein]]
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[[Category: Ribosome]]
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[[Category: Translation]]
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[[Category: Trna]]
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Conformation of EF-G during translocation

3izp

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