View source for PMID:9201917

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!align=left  |Citation
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'''Harutyunyan, EH, Oganessyan, VY, Oganessyan, NN, Avaeva, SM, Nazarova, TI, Vorobyeva, NN, Kurilova, SA, Huber, R and Mather, T'''  (1997) Crystal structure of holo inorganic pyrophosphatase from Escherichia coli at 1.9 A resolution. Mechanism of hydrolysis. ''Biochemistry'' '''36''':7754-60
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!align=left  |Abstract
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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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!align=left  |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9201917 PubMed]
Online version:[http://dx.doi.org/10.1021/bi962637u 10.1021/bi962637u]
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!align=left  |Keywords
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Binding Sites; Crystallography, X-Ray; Escherichia coli/enzymology; Hydrolysis; Inorganic Pyrophosphatase; Models, Chemical; Protein Binding; Pyrophosphatases/chemistry

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