1A6Q

CRYSTAL STRUCTURE OF THE PROTEIN SERINE/THREONINE PHOSPHATASE 2C AT 2 A RESOLUTION

Summary for 1A6Q

• Entry DOI: 10.2210/pdb1a6q/pdb
• Descriptor: PHOSPHATASE 2C, MANGANESE (II) ION, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: catalytic mechanism, metalloenzyme, protein phosphatase 2c, signal transductuin, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : P35813
• Total number of polymer chains: 1
• Total formula weight: 42707.55

Authors

Das, A.K.,Helps, N.R.,Cohen, P.T.W.,Barford, D. (deposition date: 1998-02-27, release date: 1998-05-27, Last modification date: 2024-05-22)

Primary citation

Das, A.K.,Helps, N.R.,Cohen, P.T.,Barford, D.
Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution.
EMBO J., 15:6798-6809, 1996

PubMed Abstract: Protein phosphatase 2C (PP2C) is a Mn2+- or Mg2+-dependent protein Ser/Thr phosphatase that is essential for regulating cellular stress responses in eukaryotes. The crystal structure of human PP2C reveals a novel protein fold with a catalytic domain composed of a central beta-sandwich that binds two manganese ions, which is surrounded by alpha-helices. Mn2+-bound water molecules at the binuclear metal centre coordinate the phosphate group of the substrate and provide a nucleophile and general acid in the dephosphorylation reaction. Our model presents a framework for understanding not only the classical Mn2+/Mg2+-dependent protein phosphatases but also the sequence-related domains of mitochondrial pyruvate dehydrogenase phosphatase, the Bacillus subtilus phosphatase SpoIIE and a 300-residue domain within yeast adenyl cyclase. The protein architecture and deduced catalytic mechanism are strikingly similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity, suggestive of convergent evolution of protein Ser/Thr phosphatases.

PubMed: 9003755

Experimental method

X-RAY DIFFRACTION (2 Å)