2om7

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[[Image:2om7.jpg|left|200px]]
 
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==Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-bound Elongation Factors==
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The line below this paragraph, containing "STRUCTURE_2om7", creates the "Structure Box" on the page.
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<SX load='2om7' size='340' side='right' viewer='molstar' caption='[[2om7]], [[Resolution|resolution]] 7.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2om7]] is a 10 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=2OM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OM7 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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, [[Resolution|Resolution]] 7.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4SU:4-THIOURIDINE-5-MONOPHOSPHATE'>4SU</scene>, <scene name='pdbligand=5MC:5-METHYLCYTIDINE-5-MONOPHOSPHATE'>5MC</scene>, <scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=H2U:5,6-DIHYDROURIDINE-5-MONOPHOSPHATE'>H2U</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene></td></tr>
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{{STRUCTURE_2om7| PDB=2om7 | SCENE= }}
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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=2om7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2om7 OCA], [https://pdbe.org/2om7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2om7 RCSB], [https://www.ebi.ac.uk/pdbsum/2om7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2om7 ProSAT], [https://www.topsan.org/Proteins/RSGI/2om7 TOPSAN]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/om/2om7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2om7 ConSurf].
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<div style="clear:both"></div>
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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) catalyzes tRNA translocation on the ribosome. Here a cryo-EM reconstruction of the 70S*EF-G ribosomal complex at 7.3 A resolution and the crystal structure of EF-G-2*GTP, an EF-G homolog, at 2.2 A resolution are presented. EF-G-2*GTP is structurally distinct from previous EF-G structures, and in the context of the cryo-EM structure, the conformational changes are associated with ribosome binding and activation of the GTP binding pocket. The P loop and switch II approach A2660-A2662 in helix 95 of the 23S rRNA, indicating an important role for these conserved bases. Furthermore, the ordering of the functionally important switch I and II regions, which interact with the bound GTP, is dependent on interactions with the ribosome in the ratcheted conformation. Therefore, a network of interaction with the ribosome establishes the active GTP conformation of EF-G and thus facilitates GTP hydrolysis and tRNA translocation.
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'''Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-bound Elongation Factors'''
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Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors.,Connell SR, Takemoto C, Wilson DN, Wang H, Murayama K, Terada T, Shirouzu M, Rost M, Schuler M, Giesebrecht J, Dabrowski M, Mielke T, Fucini P, Yokoyama S, Spahn CM Mol Cell. 2007 Mar 9;25(5):751-64. PMID:17349960<ref>PMID:17349960</ref>
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==Overview==
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Elongation factor G (EF-G) catalyzes tRNA translocation on the ribosome. Here a cryo-EM reconstruction of the 70S*EF-G ribosomal complex at 7.3 A resolution and the crystal structure of EF-G-2*GTP, an EF-G homolog, at 2.2 A resolution are presented. EF-G-2*GTP is structurally distinct from previous EF-G structures, and in the context of the cryo-EM structure, the conformational changes are associated with ribosome binding and activation of the GTP binding pocket. The P loop and switch II approach A2660-A2662 in helix 95 of the 23S rRNA, indicating an important role for these conserved bases. Furthermore, the ordering of the functionally important switch I and II regions, which interact with the bound GTP, is dependent on interactions with the ribosome in the ratcheted conformation. Therefore, a network of interaction with the ribosome establishes the active GTP conformation of EF-G and thus facilitates GTP hydrolysis and tRNA translocation.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2OM7 is a [[Protein complex]] structure of sequences 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=2OM7 OCA].
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</div>
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<div class="pdbe-citations 2om7" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors., Connell SR, Takemoto C, Wilson DN, Wang H, Murayama K, Terada T, Shirouzu M, Rost M, Schuler M, Giesebrecht J, Dabrowski M, Mielke T, Fucini P, Yokoyama S, Spahn CM, Mol Cell. 2007 Mar 9;25(5):751-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17349960 17349960]
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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[[Category: Protein complex]]
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*[[Ribosomal protein L1|Ribosomal protein L1]]
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*[[Ribosome 3D structures|Ribosome 3D structures]]
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*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Connell, S R.]]
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[[Category: Connell SR]]
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[[Category: Dabrowski, M.]]
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[[Category: Dabrowski M]]
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[[Category: Fucini, P.]]
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[[Category: Fucini P]]
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[[Category: Giesebrecht, J.]]
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[[Category: Giesebrecht J]]
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[[Category: Mielke, T.]]
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[[Category: Mielke T]]
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[[Category: Rost, M.]]
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[[Category: Rost M]]
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[[Category: Schueler, M.]]
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[[Category: Schueler M]]
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[[Category: Spahn, C M.T.]]
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[[Category: Spahn CMT]]
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[[Category: Wilson, D N.]]
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[[Category: Wilson DN]]
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[[Category: Ribosome]]
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[[Category: Rna-protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:12:06 2008''
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Current revision

Structural Basis for Interaction of the Ribosome with the Switch Regions of GTP-bound Elongation Factors

2om7, resolution 7.30Å

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