1jfd

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(New page: 200px<br /><applet load="1jfd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jfd, resolution 2.2&Aring;" /> '''STRUCTURE OF INORGANI...)
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[[Image:1jfd.jpg|left|200px]]<br /><applet load="1jfd" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jfd.jpg|left|200px]]<br /><applet load="1jfd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jfd, resolution 2.2&Aring;" />
caption="1jfd, resolution 2.2&Aring;" />
'''STRUCTURE OF INORGANIC PYROPHOSPHATASE'''<br />
'''STRUCTURE OF INORGANIC PYROPHOSPHATASE'''<br />
==Overview==
==Overview==
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The three-dimensional structure of inorganic pyrophosphatase from, Escherichia coli complexed with sulfate was determined at 2.2 A resolution, using Patterson's search technique and refmed to an R-factor of 19.2%., Sulfate may be regarded as a structural analog of phosphate, the product, of the enzyme reaction, and as a structural analog of methyl phosphate, the irreversible inhibitor. Sulfate binds to the pyrophosphatase active, site cavity as does phosphate and this diminishes molecular symmetry, converting the homohexamer structure form (alpha3)2 into alpha3'alpha3"., The asymmetry of the molecule is manifested in displacements of protein, functional groups and some parts of the polypeptide chain and reflects the, interaction of subunits and their cooperation. The significance of, re-arrangements for pyrophosphatase function is discussed.
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The three-dimensional structure of inorganic pyrophosphatase from Escherichia coli complexed with sulfate was determined at 2.2 A resolution using Patterson's search technique and refmed to an R-factor of 19.2%. Sulfate may be regarded as a structural analog of phosphate, the product of the enzyme reaction, and as a structural analog of methyl phosphate, the irreversible inhibitor. Sulfate binds to the pyrophosphatase active site cavity as does phosphate and this diminishes molecular symmetry, converting the homohexamer structure form (alpha3)2 into alpha3'alpha3". The asymmetry of the molecule is manifested in displacements of protein functional groups and some parts of the polypeptide chain and reflects the interaction of subunits and their cooperation. The significance of re-arrangements for pyrophosphatase function is discussed.
==About this Structure==
==About this Structure==
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1JFD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JFD OCA].
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1JFD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JFD OCA].
==Reference==
==Reference==
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[[Category: Inorganic diphosphatase]]
[[Category: Inorganic diphosphatase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Avaeva, S.M.]]
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[[Category: Avaeva, S M.]]
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[[Category: Harutyunyan, E.H.]]
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[[Category: Harutyunyan, E H.]]
[[Category: Huber, R.]]
[[Category: Huber, R.]]
[[Category: Oganesyan, V.]]
[[Category: Oganesyan, V.]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:11:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:22:05 2008''

Revision as of 11:22, 21 February 2008


1jfd, resolution 2.2Å

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STRUCTURE OF INORGANIC PYROPHOSPHATASE

Overview

The three-dimensional structure of inorganic pyrophosphatase from Escherichia coli complexed with sulfate was determined at 2.2 A resolution using Patterson's search technique and refmed to an R-factor of 19.2%. Sulfate may be regarded as a structural analog of phosphate, the product of the enzyme reaction, and as a structural analog of methyl phosphate, the irreversible inhibitor. Sulfate binds to the pyrophosphatase active site cavity as does phosphate and this diminishes molecular symmetry, converting the homohexamer structure form (alpha3)2 into alpha3'alpha3". The asymmetry of the molecule is manifested in displacements of protein functional groups and some parts of the polypeptide chain and reflects the interaction of subunits and their cooperation. The significance of re-arrangements for pyrophosphatase function is discussed.

About this Structure

1JFD is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Inorganic diphosphatase, with EC number 3.6.1.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of Escherichia coli inorganic pyrophosphatase complexed with SO4(2-). Ligand-induced molecular asymmetry., Avaeva S, Kurilova S, Nazarova T, Rodina E, Vorobyeva N, Sklyankina V, Grigorjeva O, Harutyunyan E, Oganessyan V, Wilson K, Dauter Z, Huber R, Mather T, FEBS Lett. 1997 Jun 30;410(2-3):502-8. PMID:9237692

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