1rck
From Proteopedia
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THE THREE DIMENSIONAL STRUCTURE OF GUANINE-SPECIFIC RIBONUCLEASE F1 IN SOLUTION DETERMINED BY NMR SPECTROSCOPY AND DISTANCE GEOMETRY
Overview
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.
About this Structure
1RCK is a Single protein structure of sequence from Gibberella fujikuroi. Active as Ribonuclease T(1), with EC number 3.1.27.3 Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of guanine-specific ribonuclease F1 in solution determined by NMR spectroscopy and distance geometry., Nakai T, Yoshikawa W, Nakamura H, Yoshida H, Eur J Biochem. 1992 Aug 15;208(1):41-51. PMID:1511688
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