Lanmodulin (LanM) is a theorized periplasmic protein found in <i>Methylobacterium extorquens</i> used for the binding and transport of lanthanides utilized by the bacterium as enzyme cofactors. LanM has shown great potential for engineered bioextraction of rare earth elements (REE), or lanthanides (Ln), for which the current methods of mining are challenging and energy intensive. REEs are in high demand for their applications in advanced technology including permanent magnets, fiber optics, electric car batteries, smartphones, lasers, and numerous other examples. Uncovering the exact mechanism of Ln-binding by LanM could allow for engineering a protein with higher affinity for REEs and the capability to bind a greater variety of REEs for more efficient extraction of these elements. To further reveal the function of LanM, proteins from other Methylobacterium species with similar sequences were identified, modeled using AlphaFold to compare their predicted structural similarity, and their ability to bind Ln's was determined experimentally. Additionally, machine learning models, such as HMMER, can be utilized to assess LanM and LanM-like proteins and identify novel proteins with similar function, but dissimilar sequences and protein structures to further and improve this bioextraction effort.

Assessment of novel proteins’ rare earth element binding ability

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