دورية أكاديمية
Role of the transfer ribonucleic acid (tRNA) bound magnesium ions in the charging step of aminoacylation reaction in the glutamyl tRNA synthetase and the seryl tRNA synthetase bound with cognate tRNA.
| العنوان: | Role of the transfer ribonucleic acid (tRNA) bound magnesium ions in the charging step of aminoacylation reaction in the glutamyl tRNA synthetase and the seryl tRNA synthetase bound with cognate tRNA. |
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| المؤلفون: | Saha A; Department of Chemistry, University of Kalyani, Kalyani, Nadia, West Bengal, India., Nandi N; Department of Chemistry, University of Kalyani, Kalyani, Nadia, West Bengal, India. |
| المصدر: | Journal of biomolecular structure & dynamics [J Biomol Struct Dyn] 2022 Nov; Vol. 40 (18), pp. 8538-8559. Date of Electronic Publication: 2021 Apr 24. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Taylor & Francis Country of Publication: England NLM ID: 8404176 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1538-0254 (Electronic) Linking ISSN: 07391102 NLM ISO Abbreviation: J Biomol Struct Dyn Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: June 2012- : Oxon, UK : Taylor & Francis Original Publication: Guilderland, NY : Adenine Press, [c1983- |
| مواضيع طبية MeSH: | Amino Acyl-tRNA Synthetases*/metabolism , Serine-tRNA Ligase*/chemistry, Adenosine Monophosphate/metabolism ; Amino Acids/chemistry ; Aminoacylation ; Glutamate-tRNA Ligase/chemistry ; Glutamate-tRNA Ligase/genetics ; Glutamate-tRNA Ligase/metabolism ; Ions ; Ligases/metabolism ; Magnesium ; RNA, Transfer/metabolism ; RNA, Transfer, Glu/metabolism ; RNA, Transfer, Ser/metabolism |
| مستخلص: | Aminoacylation reaction is the first step of protein biosynthesis. Transfer RNA (tRNA) is charged with an amino acid in this reaction and the reaction is catalyzed by aminoacyl tRNA synthetase enzyme (aaRS). In the present work, we use classical molecular dynamics simulation to show that the tRNA bound Mg 2+ ions significantly influence the charging step of class I Tt GluRS: Glu-AMP: tRNA Glu and class II dimeric Tt SerRS: Ser-AMP: tRNA Ser . The CCA end of the acceptor terminal is disordered in the absence of coordinated Mg 2+ ions and the CCA end can freely explore beyond the specific conformational space of the tRNA in its precharging state. A balance between the conformational disorder of the tRNA and the restriction imposed on the CCA terminal via coordination with the Mg 2+ ions is needed for the placement of the CCA terminal in a precharging state organization. This result provides a molecular-level explanation of the experimental observation that the presence of Mg 2+ ions is a necessary condition for a successful aminoacylation reaction.Communicated by Ramaswamy H. Sarma. |
| فهرسة مساهمة: | Keywords: Aminoacylation; magnesium ion; metadynamics; molecular dynamics simulation; transfer RNA |
| المشرفين على المادة: | 0 (Amino Acids) 0 (Ions) 0 (RNA, Transfer, Glu) 0 (RNA, Transfer, Ser) 415SHH325A (Adenosine Monophosphate) 9014-25-9 (RNA, Transfer) EC 6.- (Ligases) EC 6.1.1.- (Amino Acyl-tRNA Synthetases) EC 6.1.1.11 (Serine-tRNA Ligase) EC 6.1.1.17 (Glutamate-tRNA Ligase) I38ZP9992A (Magnesium) |
| تواريخ الأحداث: | Date Created: 20210426 Date Completed: 20221018 Latest Revision: 20221202 |
| رمز التحديث: | 20240628 |
| DOI: | 10.1080/07391102.2021.1914732 |
| PMID: | 33896406 |
| قاعدة البيانات: | MEDLINE |
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Full Text Finder | تدمد: | 1538-0254 |
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| DOI: | 10.1080/07391102.2021.1914732 |