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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, J., Rizkallah, P., Jin, Y., Roth, C., Miller, D. J., & Allemann, R. 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 and Crystallization Communications, 76(2), 81-85. doi:10.1107/S2053230X20001181.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-A6B1-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-A6B2-6
Genre: Journal Article

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Article.pdf (Publisher version), 755KB
 
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 Creators:
Cresser-Brown, Joel, Author
Rizkallah, Pierre, Author
Jin, Yi, Author
Roth, Christian1, Author              
Miller, David J., Author
Allemann, Rudolf K., Author
Affiliations:
1Christian Roth, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2522691              

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Free keywords: calpain expression, Hfq, chaperones, cysteine protease
 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.

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Language(s): eng - English
 Dates: 2019-02-052020
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1107/S2053230X20001181
BibTex Citekey: Cresser-Brown:rl5183
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Title: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Source Genre: Journal
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Publ. Info: Blackwell Publishing Limited
Pages: - Volume / Issue: 76 (2) Sequence Number: - Start / End Page: 81 - 85 Identifier: ISSN: 1744-3091