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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2018

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Domain swapping dissection in Thermotoga maritima arginine binding protein: How structural flexibility may compensate destabilization

Anno di pubblicazione: 2018

Autori: Smaldone, Giovanni; Berisio, Rita; Balasco, Nicole; D'Auria, Sabato; Vitagliano, Luigi; Ruggiero, Alessia

Affiliazioni autori: Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, I-80134 Napoli, Italy Institute of Food Science, CNR, Via Roma, 64 Avellino, Italy

Autori CNR:

  • NICOLE BALASCO
  • RITA BERISIO
  • SABATO D'AURIA
  • ALESSIA RUGGIERO
  • LUIGI VITAGLIANO

Lingua: inglese

Abstract: Thermotoga maritima Arginine Binding Protein (TmArgBP) is a valuable candidate for arginine biosensing in diagnostics. This protein is endowed with unusual structural properties that include an extraordinary thermal/chemical stability, a domain swapped structure that undergoes large tertiary and quaternary structural transition, and the ability to form non-canonical oligomeric species. As the intrinsic stability of TmArgBP allows for extensive protein manipulations, we here dissected its structure in two parts: its main body deprived of the swapping fragment (TmArgBP(20-233)) and the C-terminal peptide corresponding to the helical swapping element. Both elements have been characterized independently or in combination using a repertoire of biophysical/structural techniques. Present investigations clearly indicate that TmArgBP(20-233) represents a better scaffold for arginine sensing compared to the wild-type protein. Moreover, our data demonstrate that the ligand-free and the ligand-bound forms respond very differently to this helix deletion. This drastic perturbation has an important impact on the ligand-bound form of TmArgBP(20-233) stability whereas it barely affects its ligand-free state. The crystallographic structures of these forms provide a rationale to this puzzling observation. Indeed, the arginine-bound state is very rigid and virtually unchanged upon protein truncation. On the other hand, the flexible ligand-free TmArgBP(20-233) is able to adopt a novel state as a consequence of the helix deletion. Therefore, the flexibility of the ligand-free form endows this state with a remarkable robustness upon severe perturbations. In this scenario, TmArgBP dissection highlights an intriguing connection between destabilizing/stabilizing effects and the overall flexibility that could operate also in other proteins.

Lingua abstract: inglese

Pagine da: 952

Pagine a: 962

Pagine totali: 11

Rivista:

Biochimica et biophysica acta. Proteins and proteomics Elsevier
Paese di pubblicazione: Paesi Bassi
Lingua: inglese
ISSN: 1570-9639

Numero volume: 1866

Numero fascicolo: 9

DOI: 10.1016/j.bbapap.2018.05.016

Stato della pubblicazione: Published version

Indicizzato da: ISI Web of Science (WOS) [000439671800004]

Parole chiave:

  • Domain swapping
  • Biosensors
  • Argininemia diagnosis
  • Protein structure-stability
  • Calorimetry

Strutture CNR:

 
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