6MI5
NMR solution structure of lanmodulin (LanM) complexed with yttrium(III) ions
Summary for 6MI5
| Entry DOI | 10.2210/pdb6mi5/pdb |
| NMR Information | BMRB: 30515 |
| Descriptor | Lanmodulin, YTTRIUM (III) ION (2 entities in total) |
| Functional Keywords | lanthanide, ef-hand, methylotroph, periplasm, metal binding protein |
| Biological source | Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) |
| Total number of polymer chains | 1 |
| Total formula weight | 12796.49 |
| Authors | Cook, E.C.,Featherson, E.R.,Showalter, S.A.,Cotruvo Jr., J.A. (deposition date: 2018-09-19, release date: 2018-11-07, Last modification date: 2024-05-01) |
| Primary citation | Cook, E.C.,Featherston, E.R.,Showalter, S.A.,Cotruvo Jr., J.A. Structural Basis for Rare Earth Element Recognition by Methylobacterium extorquens Lanmodulin. Biochemistry, 58:120-125, 2019 Cited by PubMed Abstract: Lanmodulin (LanM) is a high-affinity lanthanide (Ln)-binding protein recently identified in Methylobacterium extorquens, a bacterium that requires Lns for the function of at least two enzymes. LanM possesses four EF-hands, metal coordination motifs generally associated with Ca binding, but it undergoes a metal-dependent conformational change with a 100 million-fold selectivity for Lns and Y over Ca. Here we present the nuclear magnetic resonance solution structure of LanM complexed with Y. This structure reveals that LanM features an unusual fusion of adjacent EF-hands, resulting in a compact fold to the best of our knowledge unique among EF-hand-containing proteins. It also supports the importance of an additional carboxylate ligand in contributing to the protein's picomolar affinity for Lns, and it suggests a role of unusual N -H···N hydrogen bonds, in which LanM's unique EF-hand proline residues are engaged, in selective Ln recognition. This work sets the stage for a detailed mechanistic understanding of LanM's Ln selectivity, which may inspire new strategies for binding, detecting, and sequestering these technologically important metals. PubMed: 30352145DOI: 10.1021/acs.biochem.8b01019 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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