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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ghosh, Amit Vishveshwara, Saraswathi |
| Description | Author Affiliation: Ghosh A ( Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.); |
| Abstract | The enzymes of the family of tRNA synthetases perform their functions with high precision by synchronously recognizing the anticodon region and the aminoacylation region, which are separated by approximately 70 A in space. This precision in function is brought about by establishing good communication paths between the two regions. We have modeled the structure of the complex consisting of Escherichia coli methionyl-tRNA synthetase (MetRS), tRNA, and the activated methionine. Molecular dynamics simulations have been performed on the modeled structure to obtain the equilibrated structure of the complex and the cross-correlations between the residues in MetRS have been evaluated. Furthermore, the network analysis on these simulated structures has been carried out to elucidate the paths of communication between the activation site and the anticodon recognition site. This study has provided the detailed paths of communication, which are consistent with experimental results. Similar studies also have been carried out on the complexes (MetRS + activated methonine) and (MetRS + tRNA) along with ligand-free native enzyme. A comparison of the paths derived from the four simulations clearly has shown that the communication path is strongly correlated and unique to the enzyme complex, which is bound to both the tRNA and the activated methionine. The details of the method of our investigation and the biological implications of the results are presented in this article. The method developed here also could be used to investigate any protein system where the function takes place through long-distance communication. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 40 |
| Volume Number | 104 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2007-10-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Methionine-tRNA Ligase Chemistry Metabolism Computer Simulation Escherichia Coli Enzymology Escherichia Coli Proteins Hydrogen Bonding Kinetics Models, Molecular Protein Conformation RNA, Transfer RNA, Transfer, Met Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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