2iw3
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Elongation factor eEF3 is an ATPase that, in addition to the two canonical | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Anand, M.]] | [[Category: Anand, M.]] | ||
| - | [[Category: Andersen, C | + | [[Category: Andersen, C B.F.]] |
| - | [[Category: Andersen, G | + | [[Category: Andersen, G R.]] |
[[Category: Balar, B.]] | [[Category: Balar, B.]] | ||
[[Category: Becker, T.]] | [[Category: Becker, T.]] | ||
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[[Category: Boesen, T.]] | [[Category: Boesen, T.]] | ||
[[Category: Halic, M.]] | [[Category: Halic, M.]] | ||
| - | [[Category: Kinzy, T | + | [[Category: Kinzy, T G.]] |
[[Category: Mielke, T.]] | [[Category: Mielke, T.]] | ||
| - | [[Category: Pedersen, J | + | [[Category: Pedersen, J S.]] |
| - | [[Category: Spahn, C | + | [[Category: Spahn, C M.T.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: translation]] | [[Category: translation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:34 2008'' |
Revision as of 15:56, 21 February 2008
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ELONGATION FACTOR 3 IN COMPLEX WITH ADP
Overview
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
2IW3 is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 17:56:34 2008
Categories: Saccharomyces cerevisiae | Single protein | 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. | ADP | SO4 | Acetylation | Atp-binding | Elongation factor | Nucleotide-binding | Phosphorylation | Protein biosynthesis | Rna-binding | Rrna-binding | Translation
