Direct visualization of phosphorylase-phosphorylase kinase complexes by scanning tunneling and atomic force microscopy.
In skeletal muscle the activation of phosphorylase b is catalyzed by phosphorylase kinase. Both enzymes occur in vivo as part of a multienzyme complex. The two enzymes have been imaged by atomic force microscopy and the results compared to those previously found by scanning tunneling microscopy. Scanning tunneling microscopy and atomic force microscopy have been used to view complexes between the activating enzyme phosphorylase kinase and its substrate phosphorylase b. Changes in the size and shape of phosphorylase kinase were observed when it bound phosphorylase b.
Edstrom
R D
RD
Department of Biochemistry, Medical School, University of Minnesota, Minneapolis 55455.
Meinke
M H
MH
Yang
X R
XR
Yang
R
R
Elings
V
V
Evans
D F
DF
D000818:Animals; D004577:Electron Probe Microanalysis / Q000379:methods; D016252:Microscopy, Scanning Tunneling / Q000379:methods; D009132:Muscles / Q000201:enzymology; D010764:Phosphorylase Kinase / Q000378:metabolism* / Q000648:ultrastructure; D010763:Phosphorylase b / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits
D010763:Phosphorylase b; D010764:Phosphorylase Kinase