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Equilibrium partially folded states of B. licheniformis\(\beta \)-lactamase

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Abstract

\(\beta \)-Lactamases (penicillinases) facilitate bacterial resistance to antibiotics and are excellent theoretical and experimental models in protein structure, dynamics and evolution. Bacillus licheniformis exo-small penicillinase (ESP) is a Class A \(\beta \)-lactamase with three tryptophan residues located one in each of its two domains and one in the interface between domains. The conformational landscape of three well-characterized ESP Trp\(\rightarrow \)Phe mutants was characterized in equilibrium unfolding experiments by measuring tryptophan fluorescence, far-UV CD, activity, hydrodynamic radius, and limited proteolysis. The Trp\(\rightarrow \)Phe substitutions had little impact on the native conformation, but changed the properties of the partially folded states populated at equilibrium. The results were interpreted in the framework of modern theories of protein folding.

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Acknowledgements

This work was supported by grants from CONICET (PIP-GI 11220130100277CO) and the Universidad Nacional de Quilmes (PP 53/1002).

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  1. Valeria A. Risso

    Present address: Departamento de Quimica Fisica, Facultad de Ciencias, University of Granada, 18071, Granada, Spain

Authors and Affiliations

  1. Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Roque Sáenz Peña 352, B1876BXD, Bernal, Buenos Aires, Argentina

    Valeria A. Risso & Mario R. Ermácora

  2. Instituto Multidisciplinario de Biología Celular, Conicet-CIC-UNLP, Calle 526 y Camino General Belgrano, B1906APO, La Plata, Buenos Aires, Argentina

    Mario R. Ermácora

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  1. Valeria A. Risso
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Correspondence to Mario R. Ermácora.

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Risso, V.A., Ermácora, M.R. Equilibrium partially folded states of B. licheniformis\(\beta \)-lactamase. Eur Biophys J 48, 341–348 (2019). https://doi.org/10.1007/s00249-019-01361-8

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  • DOI: https://doi.org/10.1007/s00249-019-01361-8

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