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1jfd

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[[Image:1jfd.jpg|left|200px]]
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{{STRUCTURE_1jfd| PDB=1jfd | SCENE= }}
{{STRUCTURE_1jfd| PDB=1jfd | SCENE= }}
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'''STRUCTURE OF INORGANIC PYROPHOSPHATASE'''
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===STRUCTURE OF INORGANIC PYROPHOSPHATASE===
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==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 line below this paragraph, {{ABSTRACT_PUBMED_9237692}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 9237692 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9237692}}
==About this Structure==
==About this Structure==
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[[Category: Acid anhydride hydrolase]]
[[Category: Acid anhydride hydrolase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:09:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:09:47 2008''

Revision as of 17:09, 1 July 2008

Image:1jfd.png

Template:STRUCTURE 1jfd

STRUCTURE OF INORGANIC PYROPHOSPHATASE

Template:ABSTRACT PUBMED 9237692

About this Structure

1JFD is a Single protein structure of sequence from Escherichia coli. 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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