1igp
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(New page: 200px<br /><applet load="1igp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1igp, resolution 2.2Å" /> '''X-RAY CRYSTALLOGRAPHI...)
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Revision as of 15:15, 20 November 2007
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X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT INORGANIC PYROPHOSPHATASE FROM ESCHERICHIA COLI
Overview
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.
About this Structure
1IGP is a Single protein structure of sequence from Escherichia coli. Active as Inorganic diphosphatase, with EC number 3.6.1.1 Full crystallographic information is available from OCA.
Reference
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
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