8SLU

Crystal structure of human STEP (PTPN5) at cryogenic temperature (100 K) and high pressure (205 MPa)

8SLU の概要

• エントリーDOI: 10.2210/pdb8slu/pdb
• 分子名称: Tyrosine-protein phosphatase non-receptor type 5, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: ptpn5, step, phosphatase, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32802.21

構造登録者

Ebrahim, A.,Guerrero, L.,Riley, B.T.,Kim, M.,Huang, Q.,Finke, A.D.,Keedy, D.A. (登録日: 2023-04-24, 公開日: 2023-06-21, 最終更新日: 2023-09-27)

主引用文献

Guerrero, L.,Ebrahim, A.,Riley, B.T.,Kim, M.,Huang, Q.,Finke, A.D.,Keedy, D.A.
Pushed to extremes: distinct effects of high temperature vs. pressure on the structure of an atypical phosphatase.
Biorxiv, 2023

PubMed Abstract: Protein function hinges on small shifts of three-dimensional structure. Elevating temperature or pressure may provide experimentally accessible insights into such shifts, but the effects of these distinct perturbations on protein structures have not been compared in atomic detail. To quantitatively explore these two axes, we report the first pair of structures at physiological temperature vs. high pressure for the same protein, STEP (PTPN5). We show that these perturbations have distinct and surprising effects on protein volume, patterns of ordered solvent, and local backbone and side-chain conformations. This includes novel interactions between key catalytic loops only at physiological temperature, and a distinct conformational ensemble for another active-site loop only at high pressure. Strikingly, in torsional space, physiological temperature shifts STEP toward previously reported active-like states, while high pressure shifts it toward a previously uncharted region. Together, our work argues that temperature and pressure are complementary, powerful, fundamental macromolecular perturbations.

PubMed: 37205580
DOI: 10.1101/2023.05.02.538097

実験手法

X-RAY DIFFRACTION (1.84 Å)