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Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action.
Rosa, Brenda; Marchetti, Marialaura; Paredi, Gianluca; Amenitsch, Heinz; Franko, Nina; Benoni, Roberto; Giabbai, Barbara; De Marino, Maria Giovanna; Mozzarelli, Andrea; Ronda, Luca; Storici, Paola; Campanini, Barbara; Bettati, Stefano.
Afiliación
  • Rosa B; Dipartimento di Medicina e Chirurgia, Università di Parma, Via Gramsci 14, 43126 Parma, Italy. brenda.rosa@studenti.unipr.it.
  • Marchetti M; Centro Interdipartimentale Biopharmanet-TEC, Università di Parma, Parco Area delle Scienze 27/A, 43124 Parma, Italy. marialaura.marchetti@unipr.it.
  • Paredi G; Centro Interdipartimentale Siteia, Università di Parma, Parco Area delle Scienze 181/A, 43124 Parma, Italy. gianluca.paredi@unipr.it.
  • Amenitsch H; Institute for Inorganic Chemistry, Graz University of Technology, Stremayrgasse 9, 8010 Graz, Austria. heinz.amenitsch@elettra.eu.
  • Franko N; Dipartimento di Scienze degli Alimenti e del Farmaco, Università di Parma, Parco Area delle Scienze 23/A, 43124 Parma, Italy. nina.franko@studenti.unipr.it.
  • Benoni R; Dipartimento di Medicina e Chirurgia, Università di Parma, Via Gramsci 14, 43126 Parma, Italy. roberto.benoni@uochb.cas.cz.
  • Giabbai B; Structural Biology Laboratory, Elettra Sincrotrone Trieste S.C.p.A., SS 14 km 163,5 in AREA Science Park-Basovizza, 34149 Trieste, Italy. barbara.giabbai@elettra.eu.
  • De Marino MG; Dipartimento di Medicina e Chirurgia, Università di Parma, Via Gramsci 14, 43126 Parma, Italy. mariagiovanna.demarino@studenti.unipr.it.
  • Mozzarelli A; Dipartimento di Scienze degli Alimenti e del Farmaco, Università di Parma, Parco Area delle Scienze 23/A, 43124 Parma, Italy. andrea.mozzarelli@unipr.it.
  • Ronda L; Istituto di Biofisica, CNR, Via Moruzzi 1, 56124 Pisa, Italy. andrea.mozzarelli@unipr.it.
  • Storici P; Dipartimento di Medicina e Chirurgia, Università di Parma, Via Gramsci 14, 43126 Parma, Italy. luca.ronda@unipr.it.
  • Campanini B; Istituto di Biofisica, CNR, Via Moruzzi 1, 56124 Pisa, Italy. luca.ronda@unipr.it.
  • Bettati S; Structural Biology Laboratory, Elettra Sincrotrone Trieste S.C.p.A., SS 14 km 163,5 in AREA Science Park-Basovizza, 34149 Trieste, Italy. paola.storici@elettra.eu.
Int J Mol Sci ; 20(20)2019 Oct 21.
Article en En | MEDLINE | ID: mdl-31640223
The formation of multienzymatic complexes allows for the fine tuning of many aspects of enzymatic functions, such as efficiency, localization, stability, and moonlighting. Here, we investigated, in solution, the structure of bacterial cysteine synthase (CS) complex. CS is formed by serine acetyltransferase (CysE) and O-acetylserine sulfhydrylase isozyme A (CysK), the enzymes that catalyze the last two steps of cysteine biosynthesis in bacteria. CysK and CysE have been proposed as potential targets for antibiotics, since cysteine and related metabolites are intimately linked to protection of bacterial cells against redox damage and to antibiotic resistance. We applied a combined approach of small-angle X-ray scattering (SAXS) spectroscopy and protein painting to obtain a model for the solution structure of CS. Protein painting allowed the identification of protein-protein interaction hotspots that were then used as constrains to model the CS quaternary assembly inside the SAXS envelope. We demonstrate that the active site entrance of CysK is involved in complex formation, as suggested by site-directed mutagenesis and functional studies. Furthermore, complex formation involves a conformational change in one CysK subunit that is likely transmitted through the dimer interface to the other subunit, with a regulatory effect. Finally, SAXS data indicate that only one active site of CysK is involved in direct interaction with CysE and unambiguously unveil the quaternary arrangement of CS.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bacterias / Cisteína Sintasa / Serina O-Acetiltransferasa Idioma: En Revista: Int J Mol Sci Año: 2019 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Suiza

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bacterias / Cisteína Sintasa / Serina O-Acetiltransferasa Idioma: En Revista: Int J Mol Sci Año: 2019 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Suiza