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Differential Substrate Recognition by Maltose Binding Proteins Influenced by Structure and Dynamics.

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Three maltose binding protein (MBP) isoforms from Thermotoga maritima were structurally and dynamically analyzed. Their distinct binding pockets and hinge-bending motions reveal evolutionary adaptations for oligosaccharide recognition and specificity.

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Area of Science:

  • Structural biology
  • Protein evolution
  • Biochemistry

Background:

  • The hyperthermophile Thermotoga maritima possesses three maltose binding protein (MBP) isoforms.
  • These isoforms exhibit varying sequence identities, presenting a model for studying the evolution of substrate specificity.
  • Understanding MBP evolution is crucial for deciphering carbohydrate-binding protein adaptation.

Purpose of the Study:

  • To elucidate the structural and dynamic mechanisms underlying substrate specificity and affinity in Thermotoga maritima MBPs (tmMBPs).
  • To compare tmMBPs with homologous proteins from Escherichia coli (ecMBP) and Thermococcus litoralis.
  • To investigate how gene duplication and sequence divergence influence protein function.

Main Methods:

  • X-ray crystallography was employed to determine the structures of tmMBP1, tmMBP2, and tmMBP3.
  • Small-angle X-ray scattering (SAXS) was used to analyze protein behavior in solution.
  • Molecular dynamics simulations provided insights into protein dynamics and substrate interactions.

Main Results:

  • tmMBP1 and tmMBP2 possess larger binding pockets than tmMBP3, accommodating larger oligosaccharides.
  • Substrate-induced hinge-bending motions were larger in tmMBP1 and tmMBP2 (~52°) compared to tmMBP3 (~35°).
  • Comparative analysis with ecMBP and T. litoralis MBP highlighted features enabling selective oligosaccharide binding.

Conclusions:

  • The structural and dynamic properties of tmMBP isoforms dictate their substrate specificity and affinity.
  • Divergence in binding pocket size and hinge-bending flexibility allows for differentiation of various oligosaccharides.
  • These findings provide insights into the evolutionary pathways of carbohydrate-binding proteins with conserved folds.