1rck
From Proteopedia
(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...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1rck.jpg|left|200px]]<br /><applet load="1rck" size=" | + | [[Image:1rck.jpg|left|200px]]<br /><applet load="1rck" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rck" /> | caption="1rck" /> | ||
'''THE THREE DIMENSIONAL STRUCTURE OF GUANINE-SPECIFIC RIBONUCLEASE F1 IN SOLUTION DETERMINED BY NMR SPECTROSCOPY AND DISTANCE GEOMETRY'''<br /> | '''THE THREE DIMENSIONAL STRUCTURE OF GUANINE-SPECIFIC RIBONUCLEASE F1 IN SOLUTION DETERMINED BY NMR SPECTROSCOPY AND DISTANCE GEOMETRY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Two-dimensional 1H-NMR studies have been performed on ribonuclease F1 | + | 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== | ==About this Structure== | ||
| - | 1RCK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gibberella_fujikuroi Gibberella fujikuroi]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http:// | + | 1RCK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gibberella_fujikuroi Gibberella fujikuroi]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCK OCA]. |
==Reference== | ==Reference== | ||
| Line 20: | Line 20: | ||
[[Category: hydrolase(endoribonuclease)]] | [[Category: hydrolase(endoribonuclease)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:25 2008'' |
Revision as of 12:49, 21 February 2008
|
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 Thu Feb 21 14:49:25 2008
