Solution structure of phosphorylase kinase studied using small-angle x-ray and neutron scattering

• Published in: Biochemistry (Easton) Vol. 31; no. 2; pp. 437 - 442
• Main Authors: Henderson, S. J, Newsholme, P, Heidorn, D. B, Mitchell, R, Seeger, P. A, Walsh, D. A, Trewhella, J
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 21.01.1992
• Subjects: 550600 - Medicine; Analytical, structural and metabolic biochemistry; ANIMALS; AQUEOUS SOLUTIONS; Biological and medical sciences; DISPERSIONS; Enzyme Activation; ENZYMES; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; GEOMETRY; MAMMALS; MATHEMATICS; MIXTURES; Models, Molecular; MOLECULAR STRUCTURE; neutron scattering; Neutrons; ORGANIC COMPOUNDS; PHOSPHORUS-GROUP TRANSFERASES; phosphorylase kinase; Phosphorylase Kinase - chemistry; Phosphorylase Kinase - radiation effects; PHOSPHOTRANSFERASES; PROTEINS; RABBITS; RADIOLOGY AND NUCLEAR MEDICINE; SCATTERING; Scattering, Radiation; skeletal muscle; SOLUTIONS; structure; Structure-Activity Relationship; TRANSFERASES; VERTEBRATES; X-Ray Diffraction; Vertebrata; Mammalia; Neutron scattering; Enzyme; Rabbit; X ray scattering; Lagomorpha; Striated muscle; Phosphorylase kinase; Structural analysis
• DOI: 10.1021/bi00117a019
• ISSN: 0006-2960

Small-angle X-ray and neutron scattering have been used to characterize the solution structure of rabbit skeletal phosphorylase kinase. The radius of gyration of the unactivated holoenzyme determined from neutron scattering is 94 A, and its maximum dimension is approximately 275-295 A. A planar model has been constructed that is in general agreement with the dimensions of the transmission electron microscope images of negatively stained phosphorylase kinase and that gives values for the radius of gyration, maximum linear dimension, and a pair distribution function for the structure that are consistent with the scattering data.