Crystal structure of active elongation factor Tu reveals major domain rearrangements

Harald Berchtold; Ludmila Reshetnikova; Christian O.A. Reiser; Norbert K. Schirmer; Mathias Sprinzl; Rolf Hilgenfeld

doi:10.1038/365126a0

Crystal structure of active elongation factor Tu reveals major domain rearrangements

Harald Berchtold, Ludmila Reshetnikova, Christian O.A. Reiser, Norbert K. Schirmer, Mathias Sprinzl, Rolf Hilgenfeld^*

^*Corresponding author for this work

Institute of Biochemistry

Universität Bayreuth

541 Citations (Scopus)

Abstract

The crystal structure of intact elongation factor Tu (EF-Tu) from Thermus thermophilus has been determined and refined at an effective resolution of 1.7 Å, with incorporation of data extending to 1.45 Å. The effector region, including interaction sites for the ribosome and for transfer RNA, is well defined. Molecular mechanisms are proposed for transductlon and amplification of the signal induced by GTP binding as well as for the intrinsic and effector-enhanced GTPase activity of EF-Tu. Comparison of the structure with that of EF-Tu-GDP reveals major mutual rearrange-ments of the three domains of the molecule.

Original language	English
Journal	Nature
Volume	365
Issue number	6442
Pages (from-to)	126-132
Number of pages	7
ISSN	0028-0836
DOIs	https://doi.org/10.1038/365126a0
Publication status	Published - 1993

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title = "Crystal structure of active elongation factor Tu reveals major domain rearrangements",

abstract = "The crystal structure of intact elongation factor Tu (EF-Tu) from Thermus thermophilus has been determined and refined at an effective resolution of 1.7 {\AA}, with incorporation of data extending to 1.45 {\AA}. The effector region, including interaction sites for the ribosome and for transfer RNA, is well defined. Molecular mechanisms are proposed for transductlon and amplification of the signal induced by GTP binding as well as for the intrinsic and effector-enhanced GTPase activity of EF-Tu. Comparison of the structure with that of EF-Tu-GDP reveals major mutual rearrange-ments of the three domains of the molecule.",

author = "Harald Berchtold and Ludmila Reshetnikova and Reiser, \{Christian O.A.\} and Schirmer, \{Norbert K.\} and Mathias Sprinzl and Rolf Hilgenfeld",

year = "1993",

doi = "10.1038/365126a0",

language = "English",

volume = "365",

pages = "126--132",

journal = "Nature",

issn = "0028-0836",

publisher = "Nature Research",

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TY - JOUR

T1 - Crystal structure of active elongation factor Tu reveals major domain rearrangements

AU - Berchtold, Harald

AU - Reshetnikova, Ludmila

AU - Reiser, Christian O.A.

AU - Schirmer, Norbert K.

AU - Sprinzl, Mathias

AU - Hilgenfeld, Rolf

PY - 1993

Y1 - 1993

N2 - The crystal structure of intact elongation factor Tu (EF-Tu) from Thermus thermophilus has been determined and refined at an effective resolution of 1.7 Å, with incorporation of data extending to 1.45 Å. The effector region, including interaction sites for the ribosome and for transfer RNA, is well defined. Molecular mechanisms are proposed for transductlon and amplification of the signal induced by GTP binding as well as for the intrinsic and effector-enhanced GTPase activity of EF-Tu. Comparison of the structure with that of EF-Tu-GDP reveals major mutual rearrange-ments of the three domains of the molecule.

AB - The crystal structure of intact elongation factor Tu (EF-Tu) from Thermus thermophilus has been determined and refined at an effective resolution of 1.7 Å, with incorporation of data extending to 1.45 Å. The effector region, including interaction sites for the ribosome and for transfer RNA, is well defined. Molecular mechanisms are proposed for transductlon and amplification of the signal induced by GTP binding as well as for the intrinsic and effector-enhanced GTPase activity of EF-Tu. Comparison of the structure with that of EF-Tu-GDP reveals major mutual rearrange-ments of the three domains of the molecule.

UR - https://www.scopus.com/pages/publications/0027179878

U2 - 10.1038/365126a0

DO - 10.1038/365126a0

M3 - Journal articles

C2 - 8371755

AN - SCOPUS:0027179878

SN - 0028-0836

VL - 365

SP - 126

EP - 132

JO - Nature

JF - Nature

IS - 6442

ER -

Crystal structure of active elongation factor Tu reveals major domain rearrangements

Abstract

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