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Crystal structure of Escherichia coli inorganic pyrophosphatase complexed with SO 4 2−
Author(s) -
Avaeva Svetlana,
Kurilova Svetlana,
Nazarova Tatjana,
Rodina Elena,
Vorobyeva Natalya,
Sklyankina Vera,
Grigorjeva Olga,
Harutyunyan Emil,
Oganessyan Vaheh,
Wilson Keith,
Dauter Zbygnew,
Huber Robert,
Mather Timothy
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00650-9
Subject(s) - inorganic pyrophosphatase , pyrophosphatase , chemistry , escherichia coli , phosphate , crystallography , molecule , crystal structure , stereochemistry , enzyme , pyrophosphate , biochemistry , organic chemistry , gene
The three‐dimensional structure of inorganic pyrophosphatase from Escherichia coli complexed with sulfate was determined at 2.2 Å resolution using Patterson's search technique and refined to an R‐factor of 19.2%. Sulfate may be regarded as a structural analog of phosphate, the product of the enzyme reaction, and as a structural analog of methyl phosphate, the irreversible inhibitor. Sulfate binds to the pyrophosphatase active site cavity as does phosphate and this diminishes molecular symmetry, converting the homohexamer structure form (α 3 ) 2 into α 3 ′α 3 ″. The asymmetry of the molecule is manifested in displacements of protein functional groups and some parts of the polypeptide chain and reflects the interaction of subunits and their cooperation. The significance of re‐arrangements for pyrophosphatase function is discussed.