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

Malgorzata Dobosz-Bartoszek; Mark H. Pinkerton; Zbyszek Otwinowski; Srinivas Chakravarthy; Dieter Söll; Paul R. Copeland; Miljan Simonović

doi:10.1038/ncomms12941

Nature Communications (Oct 2016)

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

Malgorzata Dobosz-Bartoszek,
Mark H. Pinkerton,
Zbyszek Otwinowski,
Srinivas Chakravarthy,
Dieter Söll,
Paul R. Copeland,
Miljan Simonović

Affiliations

Malgorzata Dobosz-Bartoszek: Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago
Mark H. Pinkerton: Department of Biochemistry and Molecular Biology, Rutgers—Robert Wood Johnson Medical School
Zbyszek Otwinowski: Department of Biochemistry, University of Texas Southwestern Medical Center
Srinivas Chakravarthy: Biophysics Collaborative Access Team/Illinois Institute of Technology, Sector 18ID, Advanced Photon Source
Dieter Söll: Departments of Molecular Biophysics and Biochemistry, and Chemistry, Yale University
Paul R. Copeland: Department of Biochemistry and Molecular Biology, Rutgers—Robert Wood Johnson Medical School
Miljan Simonović: Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago

DOI: https://doi.org/10.1038/ncomms12941
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 11

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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