title: Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1.
abstract: The crystal structure of mammalian protein phosphatase-1, complexed with the toxin microcystin and determined at 2.1 A resolution, reveals that it is a metalloenzyme unrelated in architecture to the tyrosine phosphatases. Two metal ions are positioned by a central beta-alpha-beta-alpha-beta scaffold at the active site, from which emanate three surface grooves that are potential binding sites for substrates and inhibitors. The carboxy terminus is positioned at the end of one of the grooves such that regulatory sequences following the domain might modulate function. The fold of the catalytic domain is expected to be closely preserved in protein phosphatases 2A and 2B (calcineurin).
authors.affiliation: Howard Hughes Medical Institute, Rockefeller University, New York, New York 10021, USA.
authors.forename: J
authors.initials: J
authors.lastname: Goldberg
authors.forename: H B
authors.initials: HB
authors.lastname: Huang
authors.forename: Y G
authors.initials: YG
authors.lastname: Kwon
authors.forename: P
authors.initials: P
authors.lastname: Greengard
authors.forename: A C
authors.initials: AC
authors.lastname: Nairn
authors.forename: J
authors.initials: J
authors.lastname: Kuriyan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D051937:Dopamine and cAMP-Regulated Phosphoprotein 32; D004926:Escherichia coli; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D008670:Metals / Q000737:chemistry; D052998:Microcystins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry; D009687:Nuclear Proteins; D010456:Peptides, Cyclic / Q000737:chemistry; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D010750:Phosphoproteins; D011487:Protein Conformation; D054645:Protein Phosphatase 1; D011506:Proteins / Q000737:chemistry; D016601:RNA-Binding Proteins; D011817:Rabbits; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
chemical_list: C087425:ANP32A protein, human; D051937:Dopamine and cAMP-Regulated Phosphoprotein 32; D047908:Intracellular Signaling Peptides and Proteins; D008670:Metals; D052998:Microcystins; D009419:Nerve Tissue Proteins; D009687:Nuclear Proteins; D010456:Peptides, Cyclic; D010750:Phosphoproteins; D011506:Proteins; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; C078588:microcystin; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1