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An unexpected co-crystal structure of the calpain PEF(S) domain with Hfq reveals a potential chaperone function of Hfq

Cresser-Brown, Joel, Rizkallah, Pierre, Jin, Yi, Roth, Christian, Miller, David J. and Allemann, Rudolf K. 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: Medicine
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: 31 Jul 2020 15:06
URI: http://orca-mwe.cf.ac.uk/id/eprint/129816

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