1FJM

Protein serine/threonine phosphatase-1 (alpha isoform, type 1) complexed with microcystin-LR toxin

Summary for 1FJM

• Entry DOI: 10.2210/pdb1fjm/pdb
• Related PRD ID: PRD_000212
• Descriptor: PROTEIN SERINE/THREONINE PHOSPHATASE-1 (ALPHA ISOFORM, TYPE 1), microcystin LR, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: hydrolase, toxin, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Oryctolagus cuniculus (rabbit); More
• Total number of polymer chains: 4
• Total formula weight: 77520.51

Authors

Goldberg, J.,Nairn, A.C.,Kuriyan, J. (deposition date: 1995-12-17, release date: 1996-06-20, Last modification date: 2023-11-15)

Primary citation

Goldberg, J.,Huang, H.B.,Kwon, Y.G.,Greengard, P.,Nairn, A.C.,Kuriyan, J.
Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1.
Nature, 376:745-753, 1995

PubMed 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).

PubMed: 7651533
DOI: 10.1038/376745a0

Experimental method

X-RAY DIFFRACTION (2.1 Å)