1rch

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(New page: 200px<br /><applet load="1rch" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rch" /> '''SOLUTION NMR STRUCTURE OF RIBONUCLEASE HI FR...)
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'''SOLUTION NMR STRUCTURE OF RIBONUCLEASE HI FROM ESCHERICHIA COLI, 8 STRUCTURES'''<br />
'''SOLUTION NMR STRUCTURE OF RIBONUCLEASE HI FROM ESCHERICHIA COLI, 8 STRUCTURES'''<br />
==Overview==
==Overview==
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The solution structure of ribonuclease HI (RNase HI) from Escherichia coli, (E. coli), a protein of 155 residues, was determined. Three-dimensional, nuclear Overhauser enhancement spectroscopy (NOESY) was used to obtain, 1,424 distance constraints between individually assigned polypeptide chain, hydrogen atoms. Supplemental geometric constraints of 90phi angles and, 12chi1 angles, and the distance constraints of 66 hydrogen bonds were, experimentally derived. Using the DADAS90 program that calculates, structures in dihedral angle space, 15 structures satisfying almost all, constraints were obtained. The average root mean square deviation (RMSD), from the mean structure was 0.75 A for backbone atoms. The RMSD for, backbone atoms between the representative NMR structure with the smallest, constraint violation and crystal structures was within 1.2 A. Although the, NMR and crystal structures thus resemble one another, a significant, discrepancy was observed in a region termed 'basic protrusion.' The, discrepancy observed in NMR experiments is explained by fluctuation in, this region.
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The solution structure of ribonuclease HI (RNase HI) from Escherichia coli (E. coli), a protein of 155 residues, was determined. Three-dimensional nuclear Overhauser enhancement spectroscopy (NOESY) was used to obtain 1,424 distance constraints between individually assigned polypeptide chain hydrogen atoms. Supplemental geometric constraints of 90phi angles and 12chi1 angles, and the distance constraints of 66 hydrogen bonds were experimentally derived. Using the DADAS90 program that calculates structures in dihedral angle space, 15 structures satisfying almost all constraints were obtained. The average root mean square deviation (RMSD) from the mean structure was 0.75 A for backbone atoms. The RMSD for backbone atoms between the representative NMR structure with the smallest constraint violation and crystal structures was within 1.2 A. Although the NMR and crystal structures thus resemble one another, a significant discrepancy was observed in a region termed 'basic protrusion.' The discrepancy observed in NMR experiments is explained by fluctuation in this region.
==About this Structure==
==About this Structure==
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1RCH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RCH OCA].
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1RCH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCH OCA].
==Reference==
==Reference==
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[[Category: nuclease]]
[[Category: nuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:22 2008''

Revision as of 12:49, 21 February 2008


1rch

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SOLUTION NMR STRUCTURE OF RIBONUCLEASE HI FROM ESCHERICHIA COLI, 8 STRUCTURES

Overview

The solution structure of ribonuclease HI (RNase HI) from Escherichia coli (E. coli), a protein of 155 residues, was determined. Three-dimensional nuclear Overhauser enhancement spectroscopy (NOESY) was used to obtain 1,424 distance constraints between individually assigned polypeptide chain hydrogen atoms. Supplemental geometric constraints of 90phi angles and 12chi1 angles, and the distance constraints of 66 hydrogen bonds were experimentally derived. Using the DADAS90 program that calculates structures in dihedral angle space, 15 structures satisfying almost all constraints were obtained. The average root mean square deviation (RMSD) from the mean structure was 0.75 A for backbone atoms. The RMSD for backbone atoms between the representative NMR structure with the smallest constraint violation and crystal structures was within 1.2 A. Although the NMR and crystal structures thus resemble one another, a significant discrepancy was observed in a region termed 'basic protrusion.' The discrepancy observed in NMR experiments is explained by fluctuation in this region.

About this Structure

1RCH is a Single protein structure of sequence from Escherichia coli. Active as Ribonuclease H, with EC number 3.1.26.4 Full crystallographic information is available from OCA.

Reference

NMR structure of ribonuclease HI from Escherichia coli., Fujiwara M, Kato T, Yamazaki T, Yamasaki K, Nagayam K, Biol Pharm Bull. 2000 Oct;23(10):1147-52. PMID:11041241

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