Pushed to extremes : distinct effects of high temperature versus pressure on the structure of STEP
© 2024. The Author(s)..
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.
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| Medienart: |
E-Artikel |
| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:7 |
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| Enthalten in: |
Communications biology - 7(2024), 1 vom: 12. Jan., Seite 59 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Guerrero, Liliana [VerfasserIn] |
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Date Completed 15.01.2024 Date Revised 10.02.2024 published: Electronic UpdateOf: bioRxiv. 2023 May 03;:. - PMID 37205580 Citation Status MEDLINE |
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| doi: |
10.1038/s42003-023-05609-0 |
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| funding: |
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NLM367072122 |
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| 245 | 1 | 0 | |a Pushed to extremes |b distinct effects of high temperature versus pressure on the structure of STEP |
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| 500 | |a Date Revised 10.02.2024 | ||
| 500 | |a published: Electronic | ||
| 500 | |a UpdateOf: bioRxiv. 2023 May 03;:. - PMID 37205580 | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a © 2024. The Author(s). | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Journal Article | |
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| 700 | 1 | |a Ebrahim, Ali |e verfasserin |4 aut | |
| 700 | 1 | |a Riley, Blake T |e verfasserin |4 aut | |
| 700 | 1 | |a Kim, Minyoung |e verfasserin |4 aut | |
| 700 | 1 | |a Huang, Qingqiu |e verfasserin |4 aut | |
| 700 | 1 | |a Finke, Aaron D |e verfasserin |4 aut | |
| 700 | 1 | |a Keedy, Daniel A |e verfasserin |4 aut | |
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