2iw3
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="2iw3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iw3, resolution 2.40Å" /> '''ELONGATION FACTOR 3...) |
|||
| (21 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2iw3.gif|left|200px]]<br /> | ||
| - | <applet load="2iw3" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2iw3, resolution 2.40Å" /> | ||
| - | '''ELONGATION FACTOR 3 IN COMPLEX WITH ADP'''<br /> | ||
| - | == | + | ==Elongation Factor 3 in complex with ADP== |
| - | Elongation factor eEF3 is an ATPase that, in addition to the two canonical | + | <StructureSection load='2iw3' size='340' side='right'caption='[[2iw3]], [[Resolution|resolution]] 2.40Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2iw3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IW3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2iwh|2iwh]], [[2ix3|2ix3]]</div></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=2iw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iw3 OCA], [https://pdbe.org/2iw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iw3 RCSB], [https://www.ebi.ac.uk/pdbsum/2iw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iw3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iw/2iw3_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2iw3 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Elongation factor eEF3 is an ATPase that, in addition to the two canonical factors eEF1A and eEF2, serves an essential function in the translation cycle of fungi. eEF3 is required for the binding of the aminoacyl-tRNA-eEF1A-GTP ternary complex to the ribosomal A-site and has been suggested to facilitate the clearance of deacyl-tRNA from the E-site. Here we present the crystal structure of Saccharomyces cerevisiae eEF3, showing that it consists of an amino-terminal HEAT repeat domain, followed by a four-helix bundle and two ABC-type ATPase domains, with a chromodomain inserted in ABC2. Moreover, we present the cryo-electron microscopy structure of the ATP-bound form of eEF3 in complex with the post-translocational-state 80S ribosome from yeast. eEF3 uses an entirely new factor binding site near the ribosomal E-site, with the chromodomain likely to stabilize the ribosomal L1 stalk in an open conformation, thus allowing tRNA release. | ||
| - | + | Structure of eEF3 and the mechanism of transfer RNA release from the E-site.,Andersen CB, Becker T, Blau M, Anand M, Halic M, Balar B, Mielke T, Boesen T, Pedersen JS, Spahn CM, Kinzy TG, Andersen GR, Beckmann R Nature. 2006 Oct 12;443(7112):663-8. Epub 2006 Aug 23. PMID:16929303<ref>PMID:16929303</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2iw3" style="background-color:#fffaf0;"></div> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ==See Also== | |
| + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Atcc 18824]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Anand, M]] | ||
| + | [[Category: Andersen, C B.F]] | ||
| + | [[Category: Andersen, G R]] | ||
| + | [[Category: Balar, B]] | ||
| + | [[Category: Becker, T]] | ||
| + | [[Category: Beckmann, R]] | ||
| + | [[Category: Blau, M]] | ||
| + | [[Category: Boesen, T]] | ||
| + | [[Category: Halic, M]] | ||
| + | [[Category: Kinzy, T G]] | ||
| + | [[Category: Mielke, T]] | ||
| + | [[Category: Pedersen, J S]] | ||
| + | [[Category: Spahn, C M.T]] | ||
| + | [[Category: Acetylation]] | ||
| + | [[Category: Atp-binding]] | ||
| + | [[Category: Elongation factor]] | ||
| + | [[Category: Nucleotide-binding]] | ||
| + | [[Category: Phosphorylation]] | ||
| + | [[Category: Protein biosynthesis]] | ||
| + | [[Category: Rna-binding]] | ||
| + | [[Category: Rrna-binding]] | ||
| + | [[Category: Translation]] | ||
Current revision
Elongation Factor 3 in complex with ADP
| |||||||||||
Categories: Atcc 18824 | Large Structures | Anand, M | Andersen, C B.F | Andersen, G R | Balar, B | Becker, T | Beckmann, R | Blau, M | Boesen, T | Halic, M | Kinzy, T G | Mielke, T | Pedersen, J S | Spahn, C M.T | Acetylation | Atp-binding | Elongation factor | Nucleotide-binding | Phosphorylation | Protein biosynthesis | Rna-binding | Rrna-binding | Translation

