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8DQ2

X-ray crystal structure of Hansschlegelia quercus lanmodulin (LanM) with lanthanum (III) bound at pH 7

Summary for 8DQ2
Entry DOI10.2210/pdb8dq2/pdb
DescriptorEF-hand domain-containing protein, LANTHANUM (III) ION, SODIUM ION, ... (5 entities in total)
Functional Keywordsmethanol dehydrogenase, metal binding protein
Biological sourceHansschlegelia quercus
Total number of polymer chains4
Total formula weight49836.26
Authors
Jung, J.J.,Lin, C.-Y.,Boal, A.K. (deposition date: 2022-07-18, release date: 2023-06-07, Last modification date: 2024-05-22)
Primary citationMattocks, 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: 37259003
DOI: 10.1038/s41586-023-05945-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

236060

數據於2025-05-14公開中

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