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Reversible domain closure modulates GlnBP ligand binding affinity.

Qun Chen1, Fang Li1, Xiaobing Zuo2

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|April 21, 2022
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Summary
This summary is machine-generated.

Glutamine binding protein (GlnBP) domain closure is vital for binding glutamine. Altering linker length affects GlnBP

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Glutamine binding protein (GlnBP) from Escherichia coli is a periplasmic protein crucial for glutamine transport.
  • GlnBP binds glutamine with high affinity (~0.1μM) and stabilizes its structure upon ligand binding.
  • The precise molecular determinants governing GlnBP's ligand binding affinity remain incompletely understood.

Purpose of the Study:

  • To investigate the role of protein domain closure dynamics in GlnBP's glutamine binding.
  • To elucidate the relationship between linker length, domain closure, and ligand binding affinity.
  • To characterize the conformational changes induced by ligand binding using biophysical techniques.

Main Methods:

  • Site-directed mutagenesis to generate GlnBP variants with altered linker lengths.
  • Isothermal titration calorimetry (ITC) to measure ligand binding affinity.
  • Small-angle X-ray scattering (SAXS) and Nuclear Magnetic Resonance (NMR) spectroscopy to monitor structural changes.

Main Results:

  • Mutants exhibited varying ligand binding affinities, directly correlating with their propensity for domain closure.
  • Domain closure movement was identified as a critical factor influencing GlnBP's binding affinity.
  • Ligand binding induces gradual ensemble conformational changes in GlnBP.

Conclusions:

  • The propensity of domain closure is a key determinant of GlnBP ligand binding affinity.
  • Structural characterization provides insights into the mechanism of glutamine binding.
  • Findings offer a structural basis for the rational design of glutamine biosensors.