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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
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Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy.

J Evenäs1, V Tugarinov, N R Skrynnikov

  • 1Protein Engineering Network Centres of Excellence, University of Toronto, Toronto, Ontario, Canada M5S 1A8.

Journal of Molecular Biology
|June 12, 2001
PubMed
Summary

Solution NMR reveals how maltodextrin-binding protein (MBP) changes shape when binding to ligands. Residual dipolar couplings precisely map domain movements, offering insights into protein dynamics and function.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Maltodextrin-binding protein (MBP) is a crucial protein involved in nutrient uptake.
  • Understanding MBP's conformational changes upon ligand binding is key to elucidating its biological function.
  • Existing data on MBP complexes provide a basis for investigating ligand-induced structural dynamics.

Purpose of the Study:

  • To investigate the structural and dynamic changes of maltodextrin-binding protein (MBP) in its ligand-free and physiologically relevant maltotriose-bound states using solution NMR.
  • To compare these solution structures with existing data for the non-physiological beta-cyclodextrin complex and corresponding crystal structures.
  • To evaluate the utility of residual dipolar couplings (RDCs) in determining domain orientations and global fold changes.

Main Methods:

  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy was employed to study MBP.
  • A large set of one-bond residual dipolar couplings (RDCs) were measured for different MBP states.
  • Structural models were generated using RDC data and X-ray crystal structures with a quasi-rigid-body domain orientation algorithm in CNS.

Main Results:

  • Domain conformations critical for biological function were investigated for ligand-free, maltotriose-bound, and beta-cyclodextrin-bound MBP.
  • Excellent agreement was observed between relative domain orientations in solution and crystal structures for ligand-free and maltotriose-bound MBP.
  • The MBP/beta-cyclodextrin complex in solution showed a ~10-degree more closed conformation compared to its crystalline state.

Conclusions:

  • Residual dipolar couplings (RDCs) are highly effective for orienting protein domains and macromolecules.
  • Ligand binding induces significant conformational changes in MBP, affecting its global fold and domain orientation.
  • Solution NMR provides valuable insights into the dynamic and structural behavior of proteins like MBP, complementing X-ray crystallography data.