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B6db references: 1962195

type Journal Article
authors Sprang SR, Withers SG, Goldsmith EJ, Fletterick RJ, Madsen NB.
title Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate
journal Science
PLP Fold Type 5
sel selected
ui 1962195
year (1991)
volume 254
number 5036
pages 1367-1371
abstract The three-dimensional structure of the activated state of glycogen phosphorylase (GP) as induced by adenosine monophosphate (AMP) has been determined from crystals of pyridoxalpyrophosphoryl-GP. The same quaternary changes relative to the inactive conformation as those induced by phosphorylation are induced by AMP, although the two regulatory signals function through different local structural mechanisms. Moreover, previous descriptions of the phosphorylase active state have been extended by demonstrating that, on activation, the amino- and carboxyl-terminal domains of GP rotate apart by 5 degrees, thereby increasing access of substrates to the catalytic site. The structure also reveals previously unobserved interactions with the nucleotide that accounts for the specificity of the nucleotide binding site for AMP in preference to inosine monophosphate.
last changed 2007/09/15 10:32

B6db references