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

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1rck.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1rck.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rck| PDB=1rck | SCENE= }}
{{STRUCTURE_1rck| PDB=1rck | SCENE= }}
-
'''THE THREE DIMENSIONAL STRUCTURE OF GUANINE-SPECIFIC RIBONUCLEASE F1 IN SOLUTION DETERMINED BY NMR SPECTROSCOPY AND DISTANCE GEOMETRY'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1511688}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1511688 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1511688}}
==About this Structure==
==About this Structure==
-
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].
+
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==
Line 26: Line 30:
[[Category: Yoshida, H.]]
[[Category: Yoshida, H.]]
[[Category: Yoshikawa, W.]]
[[Category: Yoshikawa, W.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:20:03 2008''
+
 
 +
''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

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

Page seeded by OCA on Tue Jul 29 02:51:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools