Cresser-Brown, Joel, Rizkallah, Pierre  ORCID: https://orcid.org/0000-0002-9290-0369, Jin, Yi ORCID: https://orcid.org/0000-0002-6927-4371, Roth, Christian, Miller, David J. and Allemann, Rudolf K. ORCID: https://orcid.org/0000-0002-1323-8830
2020.
An unexpected co-crystal structure of the calpain PEF(S) domain with Hfq reveals a potential chaperone function of Hfq.
Acta Crystallographica Section F: Structural Biology Communications
76
(2)
, pp. 81-85.
10.1107/S2053230X20001181
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Abstract
Calpain is a Ca2+-activated, heterodimeric cysteine protease consisting of a large catalytic subunit and a small regulatory subunit. Dysregulation of this enzyme is involved in a range of pathological conditions such as cancer, Alzheimer's disease and rheumatoid arthritis, and thus calpain I is a drug target with potential therapeutic applications. Difficulty in the production of this enzyme has hindered structural and functional investigations in the past, although heterodimeric calpain I can be generated by Escherichia coli expression in low yield. Here, an unexpected structure discovered during crystallization trials of heterodimeric calpain I (CAPN1C115S + CAPNS1ΔGR) is reported. A novel co-crystal structure of the PEF(S) domain from the dissociated regulatory small subunit of calpain I and the RNA-binding chaperone Hfq, which was likely to be overproduced as a stress response to the recombinant expression conditions, was obtained, providing unexpected insight in the chaperone function of Hfq.
| Item Type: | Article |
|---|---|
| Date Type: | Publication |
| Status: | Published |
| Schools: | Schools > Medicine Schools > Chemistry |
| Publisher: | International Union of Crystallography |
| ISSN: | 2053-230X |
| Date of First Compliant Deposit: | 19 February 2020 |
| Date of Acceptance: | 28 January 2020 |
| Last Modified: | 06 Jan 2024 02:24 |
| URI: | https://orca.cardiff.ac.uk/id/eprint/129816 |
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