9C8Y

X-ray crystal structure of Methylorubrum extorquens Ce(III)-bound LanD

9C8Y の概要

• エントリーDOI: 10.2210/pdb9c8y/pdb
• 分子名称: landiscernin, CERIUM (III) ION (3 entities in total)
• 機能のキーワード: lanthanide, cerium, methanol dehydrogenase, chaperone, metal binding protein
• 由来する生物種: Methylorubrum extorquens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6742.66

構造登録者

Jung, J.J.,Lin, C.-Y.,Boal, A.K. (登録日: 2024-06-13, 公開日: 2024-10-16, 最終更新日: 2024-11-13)

主引用文献

Larrinaga, W.B.,Jung, J.J.,Lin, C.Y.,Boal, A.K.,Cotruvo Jr., J.A.
Modulating metal-centered dimerization of a lanthanide chaperone protein for separation of light lanthanides.
Proc.Natl.Acad.Sci.USA, 121:e2410926121-e2410926121, 2024

PubMed Abstract: Elucidating details of biology's selective uptake and trafficking of rare earth elements, particularly the lanthanides, has the potential to inspire sustainable biomolecular separations of these essential metals for myriad modern technologies. Here, we biochemically and structurally characterize () LanD, a periplasmic protein from a bacterial gene cluster for lanthanide uptake. This protein provides only four ligands at its surface-exposed lanthanide-binding site, allowing for metal-centered protein dimerization that favors the largest lanthanide, La. However, the monomer prefers Nd and Sm, which are disfavored lanthanides for cellular utilization. Structure-guided mutagenesis of a metal-ligand and an outer-sphere residue weakens metal binding to the LanD monomer and enhances dimerization for Pr and Nd by 100-fold. Selective dimerization enriches high-value Pr and Nd relative to low-value La and Ce in an all-aqueous process, achieving higher separation factors than lanmodulins and comparable or better separation factors than common industrial extractants. Finally, we show that LanD interacts with lanmodulin (LanM), a previously characterized periplasmic protein that shares LanD's preference for Nd and Sm. Our results suggest that LanD's unusual metal-binding site transfers less-desirable lanthanides to LanM to siphon them away from the pathway for cytosolic import. The properties of LanD show how relatively weak chelators can achieve high selectivity, and they form the basis for the design of protein dimers for separation of adjacent lanthanide pairs and other metal ions.

PubMed: 39467132
DOI: 10.1073/pnas.2410926121

実験手法

X-RAY DIFFRACTION (1.8 Å)