2iwh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:30, 9 May 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2iwh.gif|left|200px]]<br />
 
-
<applet load="2iwh" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2iwh, resolution 3.00&Aring;" />
 
-
'''STRUCTURE OF YEAST ELONGATION FACTOR 3 IN COMPLEX WITH ADPNP'''<br />
 
-
==Overview==
+
==Structure of yeast Elongation Factor 3 in complex with ADPNP==
-
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.
+
<StructureSection load='2iwh' size='340' side='right'caption='[[2iwh]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2iwh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IWH FirstGlance]. <br>
 +
</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&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2iwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwh OCA], [https://pdbe.org/2iwh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iwh RCSB], [https://www.ebi.ac.uk/pdbsum/2iwh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iwh ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/EF3A_YEAST EF3A_YEAST] Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis. Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied.<ref>PMID:6456269</ref> <ref>PMID:7657623</ref>
 +
== 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/2iwh_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=2iwh 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.
-
==About this Structure==
+
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>
-
2IWH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IWH OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16929303 16929303]
+
</div>
-
[[Category: Saccharomyces cerevisiae]]
+
<div class="pdbe-citations 2iwh" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[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: ANP]]
+
-
[[Category: SO4]]
+
-
[[Category: acetylation]]
+
-
[[Category: atp-binding]]
+
-
[[Category: elongation factor]]
+
-
[[Category: nucleotide-binding]]
+
-
[[Category: phosphorylation]]
+
-
[[Category: protein biosynthesis]]
+
-
[[Category: rna-binding]]
+
-
[[Category: rrna-binding]]
+
-
[[Category: translation]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 18:18:45 2007''
+
==See Also==
 +
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Saccharomyces cerevisiae]]
 +
[[Category: Anand M]]
 +
[[Category: Andersen CBF]]
 +
[[Category: Andersen GR]]
 +
[[Category: Balar B]]
 +
[[Category: Becker T]]
 +
[[Category: Beckmann R]]
 +
[[Category: Blau M]]
 +
[[Category: Boesen T]]
 +
[[Category: Halic M]]
 +
[[Category: Kinzy TG]]
 +
[[Category: Mielke T]]
 +
[[Category: Pedersen JS]]
 +
[[Category: Spahn CMT]]

Current revision

Structure of yeast Elongation Factor 3 in complex with ADPNP

PDB ID 2iwh

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools