1RCK

THE THREE DIMENSIONAL STRUCTURE OF GUANINE-SPECIFIC RIBONUCLEASE F1 IN SOLUTION DETERMINED BY NMR SPECTROSCOPY AND DISTANCE GEOMETRY

1RCK の概要

• エントリーDOI: 10.2210/pdb1rck/pdb
• 分子名称: RIBONUCLEASE F1 (1 entity in total)
• 機能のキーワード: hydrolase(endoribonuclease)
• 由来する生物種: Gibberella fujikuroi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10989.54

構造登録者

Nakai, T.,Yoshikawa, W.,Nakamura, H.,Yoshida, H. (登録日: 1994-08-08, 公開日: 1994-11-30, 最終更新日: 2024-11-20)

主引用文献

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

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: 1511688
DOI: 10.1111/j.1432-1033.1992.tb17157.x

実験手法

SOLUTION NMR