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

Christian Brix Folsted Andersen; T. Becker; M. Blau; M. Anand; M. Halic; B. Balar; T. Mielke; Thomas Boesen; Jan Skov Pedersen; C.M.T. Spahn; T.G. Kinzy; Gregers Rom Andersen; R. Beckmann

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

Christian Brix Folsted Andersen, T. Becker, M. Blau, M. Anand, M. Halic, B. Balar, T. Mielke, Thomas Boesen, Jan Skov Pedersen, C.M.T. Spahn, T.G. Kinzy, Gregers Rom Andersen, R. Beckmann

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

126 Citationer (Scopus)

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.

Originalsprog	Engelsk
Tidsskrift	Nature
Vol/bind	443
Sider (fra-til)	663-668
Antal sider	6
ISSN	0028-0836
Status	Udgivet - 2006

Citationsformater

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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.",

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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",

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volume = "443",

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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

SN - 0028-0836

VL - 443

SP - 663

EP - 668

JO - Nature

JF - Nature

ER -

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

Abstract

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