Small-angle X-ray scattering studies on yeast inorganic pyrophosphatase and its interactions with divalent metal ions, inorganic phosphate, and hydroxymethane bisphosphonate
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/sup 2 +/ and Mn/sup 2 +/) and with phosphoryl ligands (inorganic phosphate (P/sub 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/sup 2 +/ and high P/sub i/ concentration, although neither Mg/sup 2 +/ nor P/sub i/ added separately induced any measurable conformational changes. By contrast, simultaneous addition of Mn/sup 2 +/ and P/sub 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/sup 2 +/ ions and PCHOHP. The significance of the structural changes seen in PPase under various conditions is discussed. 21 references, 3 figures, 1 table.
- Research Organization:
- Argonne National Lab., IL
- DOE Contract Number:
- W-31-109-ENG-38
- OSTI ID:
- 5999724
- Journal Information:
- Biopolymers; (United States), Vol. 23
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
MAGNESIUM COMPOUNDS
BIOLOGICAL EFFECTS
MANGANESE COMPOUNDS
ORGANIC PHOSPHORUS COMPOUNDS
PHOSPHATASES
BIOCHEMICAL REACTION KINETICS
X-RAY DIFFRACTION
CATIONS
EXPERIMENTAL DATA
LIGANDS
MOLECULAR STRUCTURE
MORPHOLOGICAL CHANGES
PHOSPHATES
VALENCE
YEASTS
ALKALINE EARTH METAL COMPOUNDS
CHARGED PARTICLES
COHERENT SCATTERING
DATA
DIFFRACTION
ENZYMES
ESTERASES
FUNGI
HYDROLASES
INFORMATION
IONS
KINETICS
MICROORGANISMS
NUMERICAL DATA
ORGANIC COMPOUNDS
OXYGEN COMPOUNDS
PHOSPHORUS COMPOUNDS
PLANTS
REACTION KINETICS
SCATTERING
TRANSITION ELEMENT COMPOUNDS
550201* - Biochemistry- Tracer Techniques