Computationally derived structural insights into Rare Earth selectivity in lanmodulin and its variants.

ABSTRACT: Understanding rare earth element (REE) binding to proteins enables the engineering of selective protein-based ligands for precise REE recovery. Lanmodulin (LanM), with notable REE selectivity and picomolar binding affinity, is a promising candidate. This study shows that LanM variants employ distinct inter-residue interactions for REE binding. We detail the thermodynamics and structural aspects of binding events in wild-type (WT) Methylorubrum extorquens LanM and five EF-hand residue variants (4P₂A and 4D₉X, X = N, A, H, M), using protein variant structure prediction, molecular dynamics simulations and binding motif exploration. We demonstrate strong agreement between experimental binding measurements (apparent K _d ) and in silico

SUBMITTER: Sajeevan KA 

PROVIDER: S-EPMC11879702 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature