1RCL
THE THREE DIMENSIONAL STRUCTURE OF GUANINE-SPECIFIC RIBONUCLEASE F1 IN SOLUTION DETERMINED BY NMR SPECTROSCOPY AND DISTANCE GEOMETRY
Summary for 1RCL
| Entry DOI | 10.2210/pdb1rcl/pdb |
| Descriptor | RIBONUCLEASE F1 (1 entity in total) |
| Functional Keywords | hydrolase(endoribonuclease) |
| Biological source | Gibberella fujikuroi |
| Total number of polymer chains | 1 |
| Total formula weight | 10989.54 |
| Authors | Nakai, T.,Yoshikawa, W.,Nakamura, H.,Yoshida, H. (deposition date: 1994-08-08, release date: 1994-11-30, Last modification date: 2024-11-06) |
| Primary citation | Nakai, T.,Yoshikawa, W.,Nakamura, H.,Yoshida, H. The three-dimensional structure of guanine-specific ribonuclease F1 in solution determined by NMR spectroscopy and distance geometry. Eur.J.Biochem., 208:41-51, 1992 Cited by PubMed Abstract: Two-dimensional 1H-NMR studies have been performed on ribonuclease F1 (RNase F1), which contains 106 amino acid residues. Sequence-specific resonance assignments were accomplished for the backbone protons of 99 amino acid residues and for most of their side-chain protons. The three-dimensional structures were constructed on the basis of 820 interproton-distance restraints derived from NOE, 64 distance restraints for 32 hydrogen bonds and 33 phi torsion-angle restraints. A total of 40 structures were obtained by distance geometry and simulated-annealing calculations. The average root-mean-square deviation (residues 1-106) between the 40 converged structures and the mean structure obtained by averaging their coordinates was 0.116 +/- 0.018 nm for the backbone atoms and 0.182 +/- 0.015 nm for all atoms including the hydrogen atoms. RNase F1 was determined to be an alpha/beta-type protein. A well-defined structure constitutes the core region, which consists of a small N-terminal beta-sheet (beta 1, beta 2) and a central five-stranded beta-sheet (beta 3-beta 7) packed on a long helix. The structure of RNase F1 has been compared with that of RNase T1, which was determined by X-ray crystallography. Both belong to the same family of microbial ribonucleases. The polypeptide backbone fold of RNase F1 is basically identical to that of RNase T1. The conformation-dependent chemical shifts of the C alpha protons are well conserved between RNase F1 and RNase T1. The residues implicated in catalysis are all located on the central beta-sheet in a geometry similar to that of RNase T1. PubMed: 1511688DOI: 10.1111/j.1432-1033.1992.tb17157.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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