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Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system
Umeå University, Faculty of Science and Technology, Department of Chemistry.ORCID iD: 0000-0002-5636-2567
Umeå University, Faculty of Science and Technology, Department of Chemistry.ORCID iD: 0000-0002-4480-1219
Umeå University, Faculty of Medicine, Department of Clinical Microbiology.ORCID iD: 0000-0001-8773-7598
Umeå University, Faculty of Medicine, Department of Clinical Microbiology.ORCID iD: 0000-0002-0768-8405
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2022 (English)In: Biomolecular NMR Assignments, ISSN 1874-2718, E-ISSN 1874-270X, Vol. 16, p. 75-79Article in journal (Refereed) Published
Abstract [en]

The Hsp100 family member ClpB is a protein disaggregase which solubilizes and reactivates stress-induced protein aggregates in cooperation with the DnaK/Hsp70 chaperone system. In the pathogenic bacterium Francisella tularensis, ClpB is involved in type VI secretion system (T6SS) disassembly through depolymerization of the IglA-IglB sheath. This leads to recycling and reassembly of T6SS components and this process is essential for the virulence of the bacterium. Here we report the backbone chemical shift assignments and 15N relaxation-based backbone dynamics of the N-terminal substrate-binding domain of ClpB (1-156).

Place, publisher, year, edition, pages
Springer, 2022. Vol. 16, p. 75-79
Keywords [en]
15N relaxation, ClpB chaperone, Francisella tularensis, NMR resonance assignment, Type VI secretion system
National Category
Structural Biology
Identifiers
URN: urn:nbn:se:umu:diva-191275DOI: 10.1007/s12104-021-10062-3ISI: 000739320300001PubMedID: 34985724Scopus ID: 2-s2.0-85122286521OAI: oai:DiVA.org:umu-191275DiVA, id: diva2:1627369
Funder
Swedish Research CouncilSwedish Cancer SocietyThe Kempe FoundationsKnut and Alice Wallenberg FoundationAvailable from: 2022-01-13 Created: 2022-01-13 Last updated: 2023-03-24Bibliographically approved

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Ul Mushtaq, AmeeqÅdén, JörgenAlam, AtharSjöstedt, AndersGröbner, Gerhard

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Ul Mushtaq, AmeeqÅdén, JörgenAlam, AtharSjöstedt, AndersGröbner, Gerhard
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Department of ChemistryDepartment of Clinical Microbiology
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