D-trehalose/D-maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis: The binding of trehalose and maltose results in different protein conformational states

Petr Herman, Maria Staiano, Anna Marabotti, Antonio Varriale, Andrea Scirè, Fabio Tanfani, Jaroslav Vecer, [No Value] Mose'Rossi, Sabato D'Auria

Research output: Contribution to journalArticle

Abstract

In this work, we used fluorescence spectroscopy, molecular dynamics simulation, and Fourier transform infrared spectroscopy for investigating the effect of trehalose binding and maltose binding on the structural properties and the physical parameters of the recombinant D-trehalose/D-maltose binding protein (TMBP) from the hyperthermophilic archaeon Thermococcus litoralis. The binding of the two sugars to TMBP was studied in the temperature range 20°-100°C. The results show that TMBP possesses remarkable temperature stability and its secondary structure does not melt up to 90°C. Although both the secondary structure itself and the sequence of melting events were not significantly affected by the sugar binding, the protein assumes different conformations with different physical properties depending whether maltose or trehalose is bound to the protein. At low and moderate temperatures, TMBP possesses a structure that is highly compact both in the absence and in the presence of two sugars. At about 90°C, the structure of the unliganded TMBP partially relaxes whereas both the TMBP/maltose and the TMBP/trehalose complexes remain in the compact state. In addition, Fourier transform infrared results show that the population of α-helices exposed to the solvent was smaller in the absence than in the presence of the two sugars. The spectroscopic results are supported by molecular dynamics simulations. Our data on dynamics and stability of TMBP can contribute to a better understanding of transport-related functions of TMBP and constitute ground for targeted modifications of this protein for potential biotechnological applications.

Original languageEnglish
Pages (from-to)754-767
Number of pages14
JournalProteins: Structure, Function and Genetics
Volume63
Issue number4
DOIs
Publication statusPublished - Jun 1 2006

Fingerprint

Thermococcus
Maltose-Binding Proteins
Trehalose
Maltose
Archaea
Proteins
Sugars
Molecular Dynamics Simulation
Temperature
Molecular dynamics
Fluorescence Spectrometry
Computer simulation
Fluorescence spectroscopy
Fourier Analysis
Fourier Transform Infrared Spectroscopy
Freezing

Keywords

  • Bidimensional infrared spectroscopy
  • Biosensors
  • FTIR
  • Molecular dynamics simulations
  • Periplasmic protein
  • Trehalose/maltose-binding protein
  • Tryptophan fluorescence

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

D-trehalose/D-maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis : The binding of trehalose and maltose results in different protein conformational states. / Herman, Petr; Staiano, Maria; Marabotti, Anna; Varriale, Antonio; Scirè, Andrea; Tanfani, Fabio; Vecer, Jaroslav; Mose'Rossi, [No Value]; D'Auria, Sabato.

In: Proteins: Structure, Function and Genetics, Vol. 63, No. 4, 01.06.2006, p. 754-767.

Research output: Contribution to journalArticle

Herman, Petr ; Staiano, Maria ; Marabotti, Anna ; Varriale, Antonio ; Scirè, Andrea ; Tanfani, Fabio ; Vecer, Jaroslav ; Mose'Rossi, [No Value] ; D'Auria, Sabato. / D-trehalose/D-maltose-binding protein from the hyperthermophilic archaeon Thermococcus litoralis : The binding of trehalose and maltose results in different protein conformational states. In: Proteins: Structure, Function and Genetics. 2006 ; Vol. 63, No. 4. pp. 754-767.
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AU - Staiano, Maria

AU - Marabotti, Anna

AU - Varriale, Antonio

AU - Scirè, Andrea

AU - Tanfani, Fabio

AU - Vecer, Jaroslav

AU - Mose'Rossi, [No Value]

AU - D'Auria, Sabato

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N2 - In this work, we used fluorescence spectroscopy, molecular dynamics simulation, and Fourier transform infrared spectroscopy for investigating the effect of trehalose binding and maltose binding on the structural properties and the physical parameters of the recombinant D-trehalose/D-maltose binding protein (TMBP) from the hyperthermophilic archaeon Thermococcus litoralis. The binding of the two sugars to TMBP was studied in the temperature range 20°-100°C. The results show that TMBP possesses remarkable temperature stability and its secondary structure does not melt up to 90°C. Although both the secondary structure itself and the sequence of melting events were not significantly affected by the sugar binding, the protein assumes different conformations with different physical properties depending whether maltose or trehalose is bound to the protein. At low and moderate temperatures, TMBP possesses a structure that is highly compact both in the absence and in the presence of two sugars. At about 90°C, the structure of the unliganded TMBP partially relaxes whereas both the TMBP/maltose and the TMBP/trehalose complexes remain in the compact state. In addition, Fourier transform infrared results show that the population of α-helices exposed to the solvent was smaller in the absence than in the presence of the two sugars. The spectroscopic results are supported by molecular dynamics simulations. Our data on dynamics and stability of TMBP can contribute to a better understanding of transport-related functions of TMBP and constitute ground for targeted modifications of this protein for potential biotechnological applications.

AB - In this work, we used fluorescence spectroscopy, molecular dynamics simulation, and Fourier transform infrared spectroscopy for investigating the effect of trehalose binding and maltose binding on the structural properties and the physical parameters of the recombinant D-trehalose/D-maltose binding protein (TMBP) from the hyperthermophilic archaeon Thermococcus litoralis. The binding of the two sugars to TMBP was studied in the temperature range 20°-100°C. The results show that TMBP possesses remarkable temperature stability and its secondary structure does not melt up to 90°C. Although both the secondary structure itself and the sequence of melting events were not significantly affected by the sugar binding, the protein assumes different conformations with different physical properties depending whether maltose or trehalose is bound to the protein. At low and moderate temperatures, TMBP possesses a structure that is highly compact both in the absence and in the presence of two sugars. At about 90°C, the structure of the unliganded TMBP partially relaxes whereas both the TMBP/maltose and the TMBP/trehalose complexes remain in the compact state. In addition, Fourier transform infrared results show that the population of α-helices exposed to the solvent was smaller in the absence than in the presence of the two sugars. The spectroscopic results are supported by molecular dynamics simulations. Our data on dynamics and stability of TMBP can contribute to a better understanding of transport-related functions of TMBP and constitute ground for targeted modifications of this protein for potential biotechnological applications.

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