Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
An E. coli inorganic pyrophosphatase overproducer and a method for a large-scale production of the homogeneous enzyme are described. The inorganic pyrophosphatase was crystallized in the form containing one subunit of a homohexameric molecule per asymmetric unit: space group R32, a = 110.4 A, c = 76.8 A. The electron density map to 2.5 A resolution phased with Eu- and Hg-derivatives (figure of merit, <m> = 0.51) was improved by the solvent flattening procedure (<m> = 0.77). The course of the polypeptide chain and the secondary structure elements, intersubunit contacts and positions of the active sites were characterized. Homology with S. cerevisiae inorganic pyrophosphatase structure was found.
X-ray crystallographic studies of recombinant inorganic pyrophosphatase from Escherichia coli.,Oganessyan VYu, Kurilova SA, Vorobyeva NN, Nazarova TI, Popov AN, Lebedev AA, Avaeva SM, Harutyunyan EH FEBS Lett. 1994 Jul 18;348(3):301-4. PMID:8034059[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Oganessyan VYu, Kurilova SA, Vorobyeva NN, Nazarova TI, Popov AN, Lebedev AA, Avaeva SM, Harutyunyan EH. X-ray crystallographic studies of recombinant inorganic pyrophosphatase from Escherichia coli. FEBS Lett. 1994 Jul 18;348(3):301-4. PMID:8034059
