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Structure of eEF3 and the mechanism of transfer RNA release from the E-site

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Structure of eEF3 and the mechanism of transfer RNA release from the E-site. / Andersen, Christian Brix Folsted; Becker, T.; Blau, M. et al.

In: Nature, Vol. 443, 2006, p. 663-668.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Andersen, CBF, Becker, T, Blau, M, Anand, M, Halic, M, Balar, B, Mielke, T, Boesen, T, Pedersen, JS, Spahn, CMT, Kinzy, TG, Andersen, GR & Beckmann, R 2006, 'Structure of eEF3 and the mechanism of transfer RNA release from the E-site', Nature, vol. 443, pp. 663-668.

APA

Andersen, C. B. F., Becker, T., Blau, M., Anand, M., Halic, M., Balar, B., Mielke, T., Boesen, T., Pedersen, J. S., Spahn, C. M. T., Kinzy, T. G., Andersen, G. R., & Beckmann, R. (2006). Structure of eEF3 and the mechanism of transfer RNA release from the E-site. Nature, 443, 663-668.

CBE

Andersen CBF, Becker T, Blau M, Anand M, Halic M, Balar B, Mielke T, Boesen T, Pedersen JS, Spahn CMT, et al. 2006. Structure of eEF3 and the mechanism of transfer RNA release from the E-site. Nature. 443:663-668.

MLA

Vancouver

Andersen CBF, Becker T, Blau M, Anand M, Halic M, Balar B et al. Structure of eEF3 and the mechanism of transfer RNA release from the E-site. Nature. 2006;443:663-668.

Author

Andersen, Christian Brix Folsted ; Becker, T. ; Blau, M. et al. / Structure of eEF3 and the mechanism of transfer RNA release from the E-site. In: Nature. 2006 ; Vol. 443. pp. 663-668.

Bibtex

@article{07877700c66011dbbee902004c4f4f50,
title = "Structure of eEF3 and the mechanism of transfer RNA release from the E-site",
abstract = "Elongation factor eEF3 is an ATPase, which, 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 aatRNA-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 eEF3 showing that it consists of an N-terminal HEAT repeat domain, followed by a four-helix bundle and two ABC-type ATPase domains with a chromo-domain inserted in ABC2. Moreover, we present the cryo-EM 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 stabilizing the ribosomal L1 stalk in an open conformation, thus, allowing tRNA release.",
keywords = "translation, ABC proteins",
author = "Andersen, {Christian Brix Folsted} and T. Becker and M. Blau and M. Anand and M. Halic and B. Balar and T. Mielke and Thomas Boesen and Pedersen, {Jan Skov} and C.M.T. Spahn and T.G. Kinzy and Andersen, {Gregers Rom} and R. Beckmann",
year = "2006",
language = "English",
volume = "443",
pages = "663--668",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Structure of eEF3 and the mechanism of transfer RNA release from the E-site

AU - Andersen, Christian Brix Folsted

AU - Becker, T.

AU - Blau, M.

AU - Anand, M.

AU - Halic, M.

AU - Balar, B.

AU - Mielke, T.

AU - Boesen, Thomas

AU - Pedersen, Jan Skov

AU - Spahn, C.M.T.

AU - Kinzy, T.G.

AU - Andersen, Gregers Rom

AU - Beckmann, R.

PY - 2006

Y1 - 2006

N2 - Elongation factor eEF3 is an ATPase, which, 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 aatRNA-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 eEF3 showing that it consists of an N-terminal HEAT repeat domain, followed by a four-helix bundle and two ABC-type ATPase domains with a chromo-domain inserted in ABC2. Moreover, we present the cryo-EM 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 stabilizing the ribosomal L1 stalk in an open conformation, thus, allowing tRNA release.

AB - Elongation factor eEF3 is an ATPase, which, 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 aatRNA-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 eEF3 showing that it consists of an N-terminal HEAT repeat domain, followed by a four-helix bundle and two ABC-type ATPase domains with a chromo-domain inserted in ABC2. Moreover, we present the cryo-EM 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 stabilizing the ribosomal L1 stalk in an open conformation, thus, allowing tRNA release.

KW - translation

KW - ABC proteins

M3 - Journal article

VL - 443

SP - 663

EP - 668

JO - Nature

JF - Nature

SN - 0028-0836

ER -