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Modular hyperthermostable bacterial endo-β-1,4-mannanase: molecular shape, flexibility and temperature-dependent

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The hyperthermostable enzyme Endo-β-1,4-mannanase (TpMan) from Thermotoga petrophila was structurally characterized for the first time. Its linker region is compact, and the enzyme exhibits flexibility and temperature-dependent conformational changes.

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Area of Science:

  • Enzymology
  • Structural Biology
  • Biophysics

Background:

  • Endo-β-1,4-mannanase (TpMan) from Thermotoga petrophila is a hyperthermostable enzyme.
  • TpMan consists of a GH5 catalytic domain linked to a carbohydrate-binding domain.
  • The three-dimensional structure and domain arrangement of TpMan remain uncharacterized.

Purpose of the Study:

  • To determine the first structural characterization of the entire TpMan enzyme.
  • To investigate the low-resolution model, dimensions, and flexibility of TpMan.
  • To understand the role of the linker in domain spatial arrangement at varying temperatures.

Main Methods:

  • Small-angle X-ray scattering (SAXS) was employed for structural characterization.
  • Three-dimensional structures of individual domains were utilized.
  • Rigid-body modeling was performed to describe preferred conformations.

Main Results:

  • The linker region of TpMan is compact and occupies a small volume.
  • TpMan exhibits molecular flexibility in solution at 20°C.
  • A temperature-driven conformational transition occurs without significant secondary structure disruption.

Conclusions:

  • The linker optimizes domain geometry for substrate interaction at high temperatures.
  • TpMan possesses a preferred conformation despite solution flexibility.
  • These findings provide a basis for future biophysical studies of TpMan.