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Lanmodulin (LanM) protein selectively binds early lanthanides using EF-hand motifs. Conserved proline residues in LanM

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinorganic Chemistry

Background:

  • Lanthanide ions are increasingly recognized for biological importance, especially early lanthanides (La³⁺-Nd³⁺).
  • Structural principles for selective lanthanide binding in proteins are not well understood.
  • Lanmodulin (LanM) is a novel protein with high affinity and selectivity for lanthanides, preferring early ones.

Purpose of the Study:

  • Investigate LanM's selectivity mechanisms for lanthanide ions.
  • Characterize binding site geometries for early and late lanthanides, and calcium.
  • Understand the role of conserved residues in LanM's metal ion recognition.

Main Methods:

  • Two-dimensional infrared (2D IR) spectroscopy.
  • Molecular dynamics (MD) simulations.
  • Analysis of LanM's EF-hand motifs and conserved proline/glycine residues.

Main Results:

  • Conserved proline residues in EF-hands constrain binding sites for strong early lanthanide coordination.
  • Proline substitution creates more flexible but less ordered binding sites.
  • Conserved glycine residues mediate local and global protein structure.

Conclusions:

  • LanM's proline residues are key to its selective binding of early lanthanides.
  • Understanding LanM's structure-function relationships can advance lanthanide-targeting synthetic biology.
  • These findings provide insights into lanthanide recognition mechanisms in biological systems.