8FNR
X-ray crystal structure of Hansschlegelia quercus lanmodulin (LanM) with dysprosium (III) bound at pH 7
Summary for 8FNR
Entry DOI | 10.2210/pdb8fnr/pdb |
Descriptor | EF-hand domain-containing protein, DYSPROSIUM ION (3 entities in total) |
Functional Keywords | methanol dehydrogenase, metal binding protein |
Biological source | Hansschlegelia quercus |
Total number of polymer chains | 4 |
Total formula weight | 49968.20 |
Authors | Jung, J.J.,Lin, C.-Y.,Boal, A.K. (deposition date: 2022-12-28, release date: 2023-06-07, Last modification date: 2024-05-22) |
Primary citation | Mattocks, J.A.,Jung, J.J.,Lin, C.Y.,Dong, Z.,Yennawar, N.H.,Featherston, E.R.,Kang-Yun, C.S.,Hamilton, T.A.,Park, D.M.,Boal, A.K.,Cotruvo Jr., J.A. Enhanced rare-earth separation with a metal-sensitive lanmodulin dimer. Nature, 618:87-93, 2023 Cited by PubMed Abstract: Technologically critical rare-earth elements are notoriously difficult to separate, owing to their subtle differences in ionic radius and coordination number. The natural lanthanide-binding protein lanmodulin (LanM) is a sustainable alternative to conventional solvent-extraction-based separation. Here we characterize a new LanM, from Hansschlegelia quercus (Hans-LanM), with an oligomeric state sensitive to rare-earth ionic radius, the lanthanum(III)-induced dimer being >100-fold tighter than the dysprosium(III)-induced dimer. X-ray crystal structures illustrate how picometre-scale differences in radius between lanthanum(III) and dysprosium(III) are propagated to Hans-LanM's quaternary structure through a carboxylate shift that rearranges a second-sphere hydrogen-bonding network. Comparison to the prototypal LanM from Methylorubrum extorquens reveals distinct metal coordination strategies, rationalizing Hans-LanM's greater selectivity within the rare-earth elements. Finally, structure-guided mutagenesis of a key residue at the Hans-LanM dimer interface modulates dimerization in solution and enables single-stage, column-based separation of a neodymium(III)/dysprosium(III) mixture to >98% individual element purities. This work showcases the natural diversity of selective lanthanide recognition motifs, and it reveals rare-earth-sensitive dimerization as a biological principle by which to tune the performance of biomolecule-based separation processes. PubMed: 37259003DOI: 10.1038/s41586-023-05945-5 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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