Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation

Specialized translation elongation factors (eEFSec and SelB) promote selenocysteine incorporation into proteins. Here, the authors report the structure of human eEFSec, examine its interactions with guanine nucleotides, and propose a non-canonical mechanism for decoding selenocysteine.

Bibliographic Details
Main Authors:	Malgorzata Dobosz-Bartoszek, Mark H. Pinkerton, Zbyszek Otwinowski, Srinivas Chakravarthy, Dieter Söll, Paul R. Copeland, Miljan Simonović
Format:	Article
Language:	English
Published:	Nature Publishing Group 2016-10-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/ncomms12941

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spelling	doaj-1bc117eaac2c4b32ae01b3db056620d12021-05-11T10:45:44ZengNature Publishing GroupNature Communications2041-17232016-10-017111110.1038/ncomms12941Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporationMalgorzata Dobosz-Bartoszek0Mark H. Pinkerton1Zbyszek Otwinowski2Srinivas Chakravarthy3Dieter Söll4Paul R. Copeland5Miljan Simonović6Department of Biochemistry and Molecular Genetics, University of Illinois at ChicagoDepartment of Biochemistry and Molecular Biology, Rutgers—Robert Wood Johnson Medical SchoolDepartment of Biochemistry, University of Texas Southwestern Medical CenterBiophysics Collaborative Access Team/Illinois Institute of Technology, Sector 18ID, Advanced Photon SourceDepartments of Molecular Biophysics and Biochemistry, and Chemistry, Yale UniversityDepartment of Biochemistry and Molecular Biology, Rutgers—Robert Wood Johnson Medical SchoolDepartment of Biochemistry and Molecular Genetics, University of Illinois at ChicagoSpecialized translation elongation factors (eEFSec and SelB) promote selenocysteine incorporation into proteins. Here, the authors report the structure of human eEFSec, examine its interactions with guanine nucleotides, and propose a non-canonical mechanism for decoding selenocysteine.https://doi.org/10.1038/ncomms12941
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Malgorzata Dobosz-Bartoszek Mark H. Pinkerton Zbyszek Otwinowski Srinivas Chakravarthy Dieter Söll Paul R. Copeland Miljan Simonović
spellingShingle	Malgorzata Dobosz-Bartoszek Mark H. Pinkerton Zbyszek Otwinowski Srinivas Chakravarthy Dieter Söll Paul R. Copeland Miljan Simonović Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation Nature Communications
author_facet	Malgorzata Dobosz-Bartoszek Mark H. Pinkerton Zbyszek Otwinowski Srinivas Chakravarthy Dieter Söll Paul R. Copeland Miljan Simonović
author_sort	Malgorzata Dobosz-Bartoszek
title	Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation
title_short	Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation
title_full	Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation
title_fullStr	Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation
title_full_unstemmed	Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation
title_sort	crystal structures of the human elongation factor eefsec suggest a non-canonical mechanism for selenocysteine incorporation
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2016-10-01
description	Specialized translation elongation factors (eEFSec and SelB) promote selenocysteine incorporation into proteins. Here, the authors report the structure of human eEFSec, examine its interactions with guanine nucleotides, and propose a non-canonical mechanism for decoding selenocysteine.
url	https://doi.org/10.1038/ncomms12941
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Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation

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