This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1rck
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1rck" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rck" /> '''THE THREE DIMENSIONAL STRUCTURE OF GUANINE-S...)
Next diff →
Revision as of 23:20, 20 November 2007
|
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
Page seeded by OCA on Wed Nov 21 01:28:09 2007
