1rck

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{{STRUCTURE_1rck| PDB=1rck | SCENE= }}
{{STRUCTURE_1rck| PDB=1rck | SCENE= }}
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'''THE THREE DIMENSIONAL STRUCTURE OF GUANINE-SPECIFIC RIBONUCLEASE F1 IN SOLUTION DETERMINED BY NMR SPECTROSCOPY AND DISTANCE GEOMETRY'''
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===THE THREE DIMENSIONAL STRUCTURE OF GUANINE-SPECIFIC RIBONUCLEASE F1 IN SOLUTION DETERMINED BY NMR SPECTROSCOPY AND DISTANCE GEOMETRY===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 1511688 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1511688}}
==About this Structure==
==About this Structure==
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1RCK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gibberella_fujikuroi Gibberella fujikuroi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCK OCA].
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1RCK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gibberella_fujikuroi Gibberella fujikuroi]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCK OCA].
==Reference==
==Reference==
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[[Category: Yoshida, H.]]
[[Category: Yoshida, H.]]
[[Category: Yoshikawa, W.]]
[[Category: Yoshikawa, W.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:20:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:51:16 2008''

Revision as of 23:51, 28 July 2008

Image:1rck.png

Template:STRUCTURE 1rck

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

Template:ABSTRACT PUBMED 1511688

About this Structure

1RCK is a Single protein structure of sequence from Gibberella fujikuroi. Full experimental 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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