Abstract
Ribonuclease T1 (RNase T1) cleaves the phosphordiester bond of RNA, specifically at the 3’ end of guanosine. monophosphates (2’- or 3’ -GMP) as well as other purine nucleotides act as inhibitors for this reaction (Takahashi and Moore, 1982). The tertiary structure of the RNase-T1 - 2’ -GMP complex was determined by X-ray crystallography (Heinemann and Saenger, 1982; Sugio et al., 1985; Arni et al., in press). The present study revealed not only the folding manner of the enzyme but also some interesting features of protein - nucleotide interactions. We report here on the investigation of the solution structure of RNase T1 and of complexes with 2’- GMP and 3’ -GMP, using 2D-NMR spectroscopy.- Using the distance parameters obtained from this study, a preliminary molecular dynamics calculation was carried out to arrive at a tertiary structure of the complexes comparable to that obtained from crystals.
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© 1988 Plenum Press, New York
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Rüterjans, H., Hoffmann, E., Schmidt, J., Simon, J. (1988). Two-Dimensional 1H-NMR Investigation of Ribonuclease T1 and the Complexes of Rnase T1 with 2’- and 3’-Guanosine Monophosphate. In: Zelinka, J., Balan, J. (eds) Metabolism and Enzymology of Nucleic Acids. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0749-5_6
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DOI: https://doi.org/10.1007/978-1-4613-0749-5_6
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