1obw

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{{STRUCTURE_1obw| PDB=1obw | 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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Crystalline holo inorganic pyrophosphatase from Escherichia coli was grown in the presence of 250 mM MgCl2. The crystal structure has been solved by Patterson search techniques and refined to an R-factor of 17.6% at 1.9 A resolution. The upper estimate of the root-mean-square error in atomic positions is 0.26 A. These crystals belong to space group P3(2)21 with unit cell dimensions a = b = 110.27 A and c = 78.17 A. The asymmetric unit contains a trimer of subunits, i.e., half of the hexameric molecule. In the central cavity of the enzyme molecule, three Mg2+ ions, each shared by two subunits of the hexamer, are found. In the active sites of two crystallographically independent subunits, two Mg2+ ions are bound. The second active site Mg2+ ion is missing in the third subunit. A mechanism of catalysis is proposed whereby a water molecule activated by a Mg2+ ion and Tyr 55 play essential roles.
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{{ABSTRACT_PUBMED_9201917}}
==About this Structure==
==About this Structure==
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[[Category: Magnesium]]
[[Category: Magnesium]]
[[Category: Metal binding]]
[[Category: Metal binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:54:30 2008''

Revision as of 01:54, 29 July 2008

Template:STRUCTURE 1obw

STRUCTURE OF INORGANIC PYROPHOSPHATASE

Template:ABSTRACT PUBMED 9201917

About this Structure

1OBW is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of holo inorganic pyrophosphatase from Escherichia coli at 1.9 A resolution. Mechanism of hydrolysis., Harutyunyan EH, Oganessyan VY, Oganessyan NN, Avaeva SM, Nazarova TI, Vorobyeva NN, Kurilova SA, Huber R, Mather T, Biochemistry. 1997 Jun 24;36(25):7754-60. PMID:9201917

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