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Small‐angle x‐ray scattering studies on yeast inorganic pyrophosphatase and its interactions with divalent metal ions, inorganic phosphate, and hydroxymethane bisphosphonate
Author(s) -
Thiyagarajan P.,
Borso C. S.,
Banerjee A.,
Cooperman B. S.
Publication year - 1984
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360230112
Subject(s) - inorganic pyrophosphatase , chemistry , pyrophosphate , divalent , phosphate , conformational change , metal ions in aqueous solution , inorganic chemistry , enzyme , metal , pyrophosphatase , crystallography , ion , yeast , stereochemistry , biochemistry , organic chemistry
Small‐angle x‐ray scattering studies have been carried out on the enzyme yeast inorganic pyrophosphatase (PPase), and its overall conformational changes on interaction with divalent metal ions (Mg 2+ and Mn 2+ ) and with phosphoryl ligands [inorganic phosphate (P i ) and hydroxymethane bisphosphonate (PCHOHP), a nonhydrolyzable inorganic pyrophosphate analog] were assessed. The enzyme undergoes an apparent reduction in size on simultaneous addition of Mg 2+ and high P i concentration, although neithough neither Mg 2+ nor P i added separately induced any measurable conformational changes. By contrast, simultaneous addition of Mn 2+ and P i to PPase does not result in an observable conformational change. However, the overall structure of the enzyme appears to enlarge in the simultaneous presence of Mn 2+ ions and PCHOHP. The significance of the structural changes seen in PPase under various conditions is discussed.