دورية أكاديمية
أعرض في EDS

Structural basis for the tRNA-dependent activation of the terminal complex of selenocysteine synthesis in humans.

التفاصيل البيبلوغرافية
العنوان: Structural basis for the tRNA-dependent activation of the terminal complex of selenocysteine synthesis in humans.
المؤلفون: Puppala AK; Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL60607, USA., Castillo Suchkou J; Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL60607, USA., French RL; Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL60607, USA., Kiernan KA; Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL60607, USA., Simonović M; Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL60607, USA.
المصدر: Nucleic acids research [Nucleic Acids Res] 2023 May 08; Vol. 51 (8), pp. 4012-4026.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: Oxford University Press Country of Publication: England NLM ID: 0411011 Publication Model: Print Cited Medium: Internet ISSN: 1362-4962 (Electronic) Linking ISSN: 03051048 NLM ISO Abbreviation: Nucleic Acids Res Subsets: MEDLINE
أسماء مطبوعة: Publication: 1992- : Oxford : Oxford University Press
Original Publication: London, Information Retrieval ltd.
مواضيع طبية MeSH: Selenocysteine*/chemistry , RNA, Transfer*, Humans ; Protein Subunits ; Crystallography, X-Ray ; Catalytic Domain
مستخلص: O-Phosphoseryl-tRNASec selenium transferase (SepSecS) catalyzes the terminal step of selenocysteine (Sec) synthesis in archaea and eukaryotes. How the Sec synthetic machinery recognizes and discriminates tRNASec from the tRNA pool is essential to the integrity of the selenoproteome. Previously, we suggested that SepSecS adopts a competent conformation that is pre-ordered for catalysis. Herein, using high-resolution X-ray crystallography, we visualized tRNA-dependent conformational changes in human SepSecS that may be a prerequisite for achieving catalytic competency. We show that tRNASec binding organizes the active sites of the catalytic protomer, while stabilizing the N- and C-termini of the non-catalytic protomer. Binding of large anions to the catalytic groove may further optimize the catalytic site for substrate binding and catalysis. Our biochemical and mutational analyses demonstrate that productive SepSecS•tRNASec complex formation is enthalpically driven and primarily governed by electrostatic interactions between the acceptor-, TΨC-, and variable arms of tRNASec and helices α1 and α14 of SepSecS. The detailed visualization of the tRNA-dependent activation of SepSecS provides a structural basis for a revised model of the terminal reaction of Sec formation in archaea and eukaryotes.
(© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.)
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معلومات مُعتمدة: R01 GM097042 United States GM NIGMS NIH HHS
المشرفين على المادة: 0CH9049VIS (Selenocysteine)
0 (Protein Subunits)
9014-25-9 (RNA, Transfer)
تواريخ الأحداث: Date Created: 20230317 Date Completed: 20230509 Latest Revision: 20230510
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC10164584
DOI: 10.1093/nar/gkad182
PMID: 36929010
قاعدة البيانات: MEDLINE
الوصف
تدمد:1362-4962
DOI:10.1093/nar/gkad182