PMID: 8955905Jan 1, 1996Paper

Conformational flexibility of tRNA: structural changes in yeast tRNA(Asp) upon binding to aspartyl-tRNA synthetase

Biochimie
B ReesD Moras

Abstract

The availability of several X-ray structures at atomic resolution of tRNA(Asp) from yeast, both in its free state and complexed with its cognate tRNA-synthetase, enables a detailed examination of the conformational changes due to interaction with the enzyme. Although the molecule conserves its general L shape, its conformation undergoes important modifications. They may be described as a bending of the two arms which brings the 3' acceptor end and the anticodon part closer together, completed by a drastic change of the anticodon loop, which puts the anticodon bases in a more exposed position, facilitating their interaction with the synthetase. The packing interactions in the crystals are also discussed. Finally, the results of protection studies by chemical probes in solution are discussed in view of the RNA-protein contacts observed in the crystals.

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Citations

Jan 1, 1996·Biochimie·R GiegéD Moras
Nov 26, 1999·Biochimica Et Biophysica Acta·R K Airas
Jun 1, 1997·Bioorganic & Medicinal Chemistry·J RudingerR Giegé
Mar 9, 2011·Proceedings of the National Academy of Sciences of the United States of America·Jie FuJoachim Frank
Sep 2, 1998·Nucleic Acids Research·M Gerstein, W Krebs
Apr 3, 2012·Theoretical Biology & Medical Modelling·Jan C Biro
Nov 26, 2009·FEBS Letters·Rebecca W AlexanderZaida Luthey-Schulten
Sep 27, 2015·Journal of Photochemistry and Photobiology. B, Biology·A SubastriC Thirunavukkarasu
Oct 3, 2007·Proteins·Jonathan J Ellis, Susan Jones
Aug 31, 2000·Annual Review of Biochemistry·M Ibba, D Soll
Aug 15, 1998·Biological Chemistry·C M Spahn, K H Nierhaus

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