1rsm

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(New page: 200px<br /><applet load="1rsm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rsm, resolution 2.0&Aring;" /> '''THE 2-ANGSTROMS RESOL...)
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'''THE 2-ANGSTROMS RESOLUTION STRUCTURE OF A THERMOSTABLE RIBONUCLEASE A CHEMICALLY CROSS-LINKED BETWEEN LYSINE RESIDUES 7 AND 41'''<br />
'''THE 2-ANGSTROMS RESOLUTION STRUCTURE OF A THERMOSTABLE RIBONUCLEASE A CHEMICALLY CROSS-LINKED BETWEEN LYSINE RESIDUES 7 AND 41'''<br />
==Overview==
==Overview==
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The crystal structure of Lys-7-(dinitrophenylene)-Lys-41-cross-linked, ribonuclease A has been determined by molecular replacement and refined by, restrained least-squares methods to an R factor of 0.18 at 2.0-A, resolution. Diffraction intensity data were collected by using a, conventional diffractometer and an x-ray area detector. Comparison of the, thermostable cross-linked protein and the native enzyme shows them to be, structurally similar, with a rms difference in backbone and side-chain, atoms of 0.52 and 1.34 A, respectively. Native and modified proteins, additionally show 35 common bound solvent sites and similar overall, temperature factor behavior, despite localized differences resulting from, cross-link introduction, altered crystal pH, or lattice interactions with, neighboring molecules. These results are discussed in the context of, proposals on the origins of thermostability in the cross-linked enzyme.
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The crystal structure of Lys-7-(dinitrophenylene)-Lys-41-cross-linked ribonuclease A has been determined by molecular replacement and refined by restrained least-squares methods to an R factor of 0.18 at 2.0-A resolution. Diffraction intensity data were collected by using a conventional diffractometer and an x-ray area detector. Comparison of the thermostable cross-linked protein and the native enzyme shows them to be structurally similar, with a rms difference in backbone and side-chain atoms of 0.52 and 1.34 A, respectively. Native and modified proteins additionally show 35 common bound solvent sites and similar overall temperature factor behavior, despite localized differences resulting from cross-link introduction, altered crystal pH, or lattice interactions with neighboring molecules. These results are discussed in the context of proposals on the origins of thermostability in the cross-linked enzyme.
==About this Structure==
==About this Structure==
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1RSM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with NIN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RSM OCA].
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1RSM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=NIN:'>NIN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RSM OCA].
==Reference==
==Reference==
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[[Category: Pancreatic ribonuclease]]
[[Category: Pancreatic ribonuclease]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Finzel, B.C.]]
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[[Category: Finzel, B C.]]
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[[Category: Ohlendorf, D.H.]]
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[[Category: Ohlendorf, D H.]]
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[[Category: Salemme, F.R.]]
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[[Category: Salemme, F R.]]
[[Category: Sheriff, S.]]
[[Category: Sheriff, S.]]
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[[Category: Weber, P.C.]]
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[[Category: Weber, P C.]]
[[Category: NIN]]
[[Category: NIN]]
[[Category: hydrolase (nucleic acid]]
[[Category: hydrolase (nucleic acid]]
[[Category: rna)]]
[[Category: rna)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:50:32 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:54:03 2008''

Revision as of 12:54, 21 February 2008


1rsm, resolution 2.0Å

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THE 2-ANGSTROMS RESOLUTION STRUCTURE OF A THERMOSTABLE RIBONUCLEASE A CHEMICALLY CROSS-LINKED BETWEEN LYSINE RESIDUES 7 AND 41

Overview

The crystal structure of Lys-7-(dinitrophenylene)-Lys-41-cross-linked ribonuclease A has been determined by molecular replacement and refined by restrained least-squares methods to an R factor of 0.18 at 2.0-A resolution. Diffraction intensity data were collected by using a conventional diffractometer and an x-ray area detector. Comparison of the thermostable cross-linked protein and the native enzyme shows them to be structurally similar, with a rms difference in backbone and side-chain atoms of 0.52 and 1.34 A, respectively. Native and modified proteins additionally show 35 common bound solvent sites and similar overall temperature factor behavior, despite localized differences resulting from cross-link introduction, altered crystal pH, or lattice interactions with neighboring molecules. These results are discussed in the context of proposals on the origins of thermostability in the cross-linked enzyme.

About this Structure

1RSM is a Single protein structure of sequence from Bos taurus with as ligand. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.

Reference

The 2-A resolution structure of a thermostable ribonuclease A chemically cross-linked between lysine residues 7 and 41., Weber PC, Sheriff S, Ohlendorf DH, Finzel BC, Salemme FR, Proc Natl Acad Sci U S A. 1985 Dec;82(24):8473-7. PMID:3936036

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