1kf8

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(New page: 200px<br /><applet load="1kf8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kf8, resolution 1.15&Aring;" /> '''Atomic resolution st...)
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'''Atomic resolution structure of RNase A at pH 8.8'''<br />
'''Atomic resolution structure of RNase A at pH 8.8'''<br />
==Overview==
==Overview==
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The diffraction pattern of protein crystals extending to atomic resolution, guarantees a very accurate picture of the molecular structure and enables, the study of subtle phenomena related to protein functionality. Six, structures of bovine pancreatic ribonuclease at the pH* values 5.2, 5.9, 6.3, 7.1, 8.0 and 8.8 and at resolution limits in the range 1.05-1.15A, have been refined. An overall description of the six structures and, several aspects, mainly regarding pH-triggered conformational changes, are, described here. Since subtle variations were expected, a thorough, validation assessment of the six refined models was first carried out., Some stereochemical parameters, such as the N[bond]C(alpha)[bond]C angle, and the pyramidalization at the carbonyl C atoms, indicate that the, standard target values and their weights typically used in refinement may, need revision. A detailed comparison of the six structures has provided, experimental evidence on the role of Lys41 in catalysis. Furthermore, insights are given into the structural effects related to the pH-dependent, binding of a sulfate anion, which mimics the phosphate group of RNA, in, the active site. Finally, the results support a number of thermodynamic, and kinetic experimental data concerning the role of the disulfide bridge, between Cys65 and Cys72 in the folding of RNase A.
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The diffraction pattern of protein crystals extending to atomic resolution guarantees a very accurate picture of the molecular structure and enables the study of subtle phenomena related to protein functionality. Six structures of bovine pancreatic ribonuclease at the pH* values 5.2, 5.9, 6.3, 7.1, 8.0 and 8.8 and at resolution limits in the range 1.05-1.15A have been refined. An overall description of the six structures and several aspects, mainly regarding pH-triggered conformational changes, are described here. Since subtle variations were expected, a thorough validation assessment of the six refined models was first carried out. Some stereochemical parameters, such as the N[bond]C(alpha)[bond]C angle and the pyramidalization at the carbonyl C atoms, indicate that the standard target values and their weights typically used in refinement may need revision. A detailed comparison of the six structures has provided experimental evidence on the role of Lys41 in catalysis. Furthermore, insights are given into the structural effects related to the pH-dependent binding of a sulfate anion, which mimics the phosphate group of RNA, in the active site. Finally, the results support a number of thermodynamic and kinetic experimental data concerning the role of the disulfide bridge between Cys65 and Cys72 in the folding of RNase A.
==About this Structure==
==About this Structure==
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1KF8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. 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=1KF8 OCA].
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1KF8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. 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=1KF8 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Berisio, R.]]
[[Category: Berisio, R.]]
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[[Category: Lamzin, V.S.]]
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[[Category: Lamzin, V S.]]
[[Category: Mazzarella, L.]]
[[Category: Mazzarella, L.]]
[[Category: Sica, F.]]
[[Category: Sica, F.]]
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[[Category: Wilson, K.S.]]
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[[Category: Wilson, K S.]]
[[Category: Zagari, A.]]
[[Category: Zagari, A.]]
[[Category: crystal]]
[[Category: crystal]]
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[[Category: titration]]
[[Category: titration]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:09:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:28 2008''

Revision as of 11:33, 21 February 2008


1kf8, resolution 1.15Å

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Atomic resolution structure of RNase A at pH 8.8

Overview

The diffraction pattern of protein crystals extending to atomic resolution guarantees a very accurate picture of the molecular structure and enables the study of subtle phenomena related to protein functionality. Six structures of bovine pancreatic ribonuclease at the pH* values 5.2, 5.9, 6.3, 7.1, 8.0 and 8.8 and at resolution limits in the range 1.05-1.15A have been refined. An overall description of the six structures and several aspects, mainly regarding pH-triggered conformational changes, are described here. Since subtle variations were expected, a thorough validation assessment of the six refined models was first carried out. Some stereochemical parameters, such as the N[bond]C(alpha)[bond]C angle and the pyramidalization at the carbonyl C atoms, indicate that the standard target values and their weights typically used in refinement may need revision. A detailed comparison of the six structures has provided experimental evidence on the role of Lys41 in catalysis. Furthermore, insights are given into the structural effects related to the pH-dependent binding of a sulfate anion, which mimics the phosphate group of RNA, in the active site. Finally, the results support a number of thermodynamic and kinetic experimental data concerning the role of the disulfide bridge between Cys65 and Cys72 in the folding of RNase A.

About this Structure

1KF8 is a Single protein structure of sequence from Bos taurus. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.

Reference

Atomic resolution structures of ribonuclease A at six pH values., Berisio R, Sica F, Lamzin VS, Wilson KS, Zagari A, Mazzarella L, Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):441-50. Epub 2002, Feb 21. PMID:11856829

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