1IGP

X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT INORGANIC PYROPHOSPHATASE FROM ESCHERICHIA COLI

Summary for 1IGP

• Entry DOI: 10.2210/pdb1igp/pdb
• Descriptor: INORGANIC PYROPHOSPHATASE (2 entities in total)
• Functional Keywords: acid anhydride hydrolase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A7A9
• Total number of polymer chains: 1
• Total formula weight: 19585.28

Authors

Oganessyan, V.Yu.,Avaeva, S.M.,Harutyunyan, E.H. (deposition date: 1994-08-01, release date: 1994-12-20, Last modification date: 2024-02-07)

Primary citation

Oganessyan, V.Y.u.,Kurilova, S.A.,Vorobyeva, N.N.,Nazarova, T.I.,Popov, A.N.,Lebedev, A.A.,Avaeva, S.M.,Harutyunyan, E.H.
X-ray crystallographic studies of recombinant inorganic pyrophosphatase from Escherichia coli.
FEBS Lett., 348:301-304, 1994

PubMed Abstract: 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, = 0.51) was improved by the solvent flattening procedure ( = 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.

PubMed: 8034059
DOI: 10.1016/0014-5793(94)00605-9

Experimental method

X-RAY DIFFRACTION (2.2 Å)