Solution Structure of Rnase T1 and Its Complexes with Nucleotides

Abstract

The solution structure of RNase T₁ and its complexes with 2′-GMP and. 3′-GMP have been investigated by combined use of 2D-NMR spectroscopy and restrained molecular dynamics calculations (MD). An analysis of the nuclear Overhauser effects (NOEs) observed indicates the presence of one a helix as well as of two antiparallel β sheets. Interaction of the nucleotides with the active site leads to changes of the backbone conformation of the amino acids involved. However, the interaction between the protein and 3′-GMP is not as strong as the interaction with 2′-GMP, possibly because of weaker binding.