8SLT

Crystal structure of human STEP (PTPN5) at physiological temperature (310 K) and ambient pressure (0.1 MPa)

8SLT の概要

• エントリーDOI: 10.2210/pdb8slt/pdb
• 分子名称: Tyrosine-protein phosphatase non-receptor type 5, SULFATE ION (3 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: 32710.11

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: 2026-02-04)

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 versus pressure on the structure of STEP.
Commun Biol, 7:59-59, 2024

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 versus. 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 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. Altogether, our work indicates that temperature and pressure are complementary, powerful, fundamental macromolecular perturbations.

PubMed: 38216663
DOI: 10.1038/s42003-023-05609-0

実験手法

X-RAY DIFFRACTION (1.96 Å)