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2ix8

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Revision as of 15:56, 24 December 2014

MODEL FOR EEF3 BOUND TO AN 80S RIBOSOME

Structural highlights

2ix8 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dasmahapatra B, Chakraburtty K. Protein synthesis in yeast. I. Purification and properties of elongation factor 3 from Saccharomyces cerevisiae. J Biol Chem. 1981 Oct 10;256(19):9999-10004. PMID:6456269
↑ Triana-Alonso FJ, Chakraburtty K, Nierhaus KH. The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor. J Biol Chem. 1995 Sep 1;270(35):20473-8. PMID:7657623
↑ 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. Structure of eEF3 and the mechanism of transfer RNA release from the E-site. Nature. 2006 Oct 12;443(7112):663-8. Epub 2006 Aug 23. PMID:16929303 doi:10.1038/nature05126

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ix8"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2ix8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IX8 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+</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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ix8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ix8 RCSB], [http://www.ebi.ac.uk/pdbsum/2ix8 PDBsum]</span></td></tr>
+<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=2ix8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ix8 RCSB], [http://www.ebi.ac.uk/pdbsum/2ix8 PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://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]]
@@ Line 32: / Line 34: @@
 </StructureSection>
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Anand, M.]]
+[[Category: Anand, M]]
-[[Category: Andersen, C B.F.]]
+[[Category: Andersen, C B.F]]
-[[Category: Andersen, G R.]]
+[[Category: Andersen, G R]]
-[[Category: Balar, B.]]
+[[Category: Balar, B]]
-[[Category: Becker, T.]]
+[[Category: Becker, T]]
-[[Category: Beckmann, R.]]
+[[Category: Beckmann, R]]
-[[Category: Blau, M.]]
+[[Category: Blau, M]]
-[[Category: Boesen, T.]]
+[[Category: Boesen, T]]
-[[Category: Halic, M.]]
+[[Category: Halic, M]]
-[[Category: Kinzy, T G.]]
+[[Category: Kinzy, T G]]
-[[Category: Mielke, T.]]
+[[Category: Mielke, T]]
-[[Category: Pedersen, J S.]]
+[[Category: Pedersen, J S]]
-[[Category: Spahn, C M.T.]]
+[[Category: Spahn, C M.T]]
 [[Category: Atp-binding]]
 [[Category: Elongation factor]]

2ix8

From Proteopedia

Revision as of 15:56, 24 December 2014

MODEL FOR EEF3 BOUND TO AN 80S RIBOSOME

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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