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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2010

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Amino acid transport in thermophiles: characterization of an arginine-binding protein in Thermotoga maritima. 2. Molecular organization and structural stability

Anno di pubblicazione: 2010

Formato: Elettronico

Autori: Scirè A.; Marabotti A.; Staiano M.; Iozzino L.; Luchansky M.S.; Der B.S.; Dattelbaum J.D.; Tanfani F.; D’'Auria S.

Affiliazioni autori: Department of Biochemistry, Biology, and Genetics, Universita` Politecnica delle Marche, Ancona, Italy Institute of Food Sciences, CNR, Avellino, Italy Laboratory for Molecular Sensing, IBP-CNR, Via Pietro Castellino, 111, 80131 Napoli, Italy Department of Chemistry, University of Richmond, Richmond, VA 23173, USA

Autori CNR:

  • SABATO D'AURIA
  • LUISA IOZZINO
  • ANNA MARABOTTI
  • MARIA STAIANO

Lingua: inglese

Abstract: ABC transport systems provide selective passage of metabolites across cell membranes and typically require the presence of a soluble binding protein with high specificity to a specific ligand. In addition to their primary role in nutrient gathering, the binding proteins associated with bacterial transport systems have been studied for their potential to serve as design scaffolds for the development of fluorescent protein biosensors. In this work, we used Fourier transform infrared spectroscopy and molecular dynamics simulations to investigate the physicochemical properties of a hyperthermophilic binding protein from Thermotoga maritima. We demonstrated preferential binding for the polar amino acid arginine and experimentally monitored the significant stabilization achieved upon binding of ligand to protein. The effect of temperature, pH, and detergent was also studied to provide a more complete picture of the protein dynamics. A protein structure model was obtained and molecular dynamic experiments were performed to investigate and couple the spectroscopic observations with specific secondary structural elements. The data determined the presence of a buried beta-sheet providing significant stability to the protein under all conditions investigated. The specific amino acid residues responsible for arginine binding were also identified. Our data on dynamics and stability will contribute to our understanding of bacterial binding protein family members and their potential biotechnological applications

Lingua abstract: inglese

Pagine da: 687

Pagine a: 698

Rivista:

Molecular bioSystems Royal Society of Chemistry,
Paese di pubblicazione: Regno Unito
Lingua: inglese
ISSN: 1742-206X

Numero volume: 6

Numero fascicolo: 4

DOI: 10.1039/b922092e

Referee: Sì: Internazionale

Indicizzato da: ISI Web of Science (WOS) [000275715000010]

Parole chiave:

  • TRANSFORM INFRARED-SPECTROSCOPY
  • GENETICALLY-ENGINEERED PROTEIN
  • COMPUTATIONAL DESIGN
  • ABC TRANSPORTERS
  • CONSTRUCTION

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