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Structural Basis for Rare Earth Element Recognition by Methylobacterium extorquens Lanmodulin.

Erik C Cook1, Emily R Featherston1, Scott A Showalter1,2

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Lanmodulin (LanM) is a unique lanthanide-binding protein. Its novel structure explains its high selectivity for lanthanides (Ln) over calcium, paving the way for metal binding and detection strategies.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Metalloprotein Chemistry

Background:

  • Lanmodulin (LanM) is a high-affinity lanthanide-binding protein from Methylobacterium extorquens.
  • LanM exhibits 100 million-fold selectivity for lanthanides (Ln) and Yttrium (Y) over Calcium (Ca).

Purpose of the Study:

  • To elucidate the structural basis of LanM's lanthanide selectivity.
  • To understand the unique metal-binding mechanism of LanM.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to determine the solution structure of LanM.
  • Structural analysis of the LanM-Yttrium (Y) complex.

Main Results:

  • Revealed an unusual fused EF-hand structure in LanM, unique among EF-hand proteins.
  • Identified the role of an additional carboxylate ligand in picomolar affinity for Ln.
  • Highlighted the contribution of unusual Ni+1-H···Ni hydrogen bonds involving proline residues to selective Ln recognition.

Conclusions:

  • The unique structure of LanM underpins its remarkable Ln selectivity.
  • This study provides a foundation for understanding LanM's mechanism and developing strategies for Ln binding and detection.