5UCG

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

5UCG の概要

• エントリーDOI: 10.2210/pdb5ucg/pdb
• 分子名称: Stage II sporulation protein E (1 entity in total)
• 機能のキーワード: ppm phosphatase, hydrolase
• 由来する生物種: Bacillus subtilis (strain 168)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 192143.61

構造登録者

Bradshaw, N.,Levdikov, V.,Zimanyi, C.,Gaudet, R.,Wilkinson, A.,Losick, R. (登録日: 2016-12-22, 公開日: 2017-05-31, 最終更新日: 2023-10-04)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.906 Å)