5UCG

Structure of the PP2C Phosphatase Domain and a Fragment of the Regulatory Domain of the Cell Fate Determinant SpoIIE from Bacillus Subtilis

Summary for 5UCG

• Entry DOI: 10.2210/pdb5ucg/pdb
• Descriptor: Stage II sporulation protein E (1 entity in total)
• Functional Keywords: ppm phosphatase, hydrolase
• Biological source: Bacillus subtilis (strain 168)
• Total number of polymer chains: 5
• Total formula weight: 192143.61

Authors

Bradshaw, N.,Levdikov, V.,Zimanyi, C.,Gaudet, R.,Wilkinson, A.,Losick, R. (deposition date: 2016-12-22, release date: 2017-05-31, Last modification date: 2023-10-04)

Primary citation

Bradshaw, N.,Levdikov, V.M.,Zimanyi, C.M.,Gaudet, R.,Wilkinson, A.J.,Losick, R.
A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases.
Elife, 6:-, 2017

PubMed Abstract: PP2C phosphatases control biological processes including stress responses, development, and cell division in all kingdoms of life. Diverse regulatory domains adapt PP2C phosphatases to specific functions, but how these domains control phosphatase activity was unknown. We present structures representing active and inactive states of the PP2C phosphatase SpoIIE from . Based on structural analyses and genetic and biochemical experiments, we identify an α-helical switch that shifts a carbonyl oxygen into the active site to coordinate a metal cofactor. Our analysis indicates that this switch is widely conserved among PP2C family members, serving as a platform to control phosphatase activity in response to diverse inputs. Remarkably, the switch is shared with proteasomal proteases, which we identify as evolutionary and structural relatives of PP2C phosphatases. Although these proteases use an unrelated catalytic mechanism, rotation of equivalent helices controls protease activity by movement of the equivalent carbonyl oxygen into the active site.

PubMed: 28527238
DOI: 10.7554/eLife.26111

Experimental method

X-RAY DIFFRACTION (3.906 Å)