Structural Basis for Rare Earth Element Recognition by Methylobacterium extorquens Lanmodulin

Erik C. Cook, Emily R. Featherston, Scott A. Showalter, Joseph A. Cotruvo

Research output: Contribution to journalArticle

14 Scopus citations

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 II binding, but it undergoes a metal-dependent conformational change with a 100 million-fold selectivity for Ln III s and Y III over Ca II . Here we present the nuclear magnetic resonance solution structure of LanM complexed with Y III . 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 Ln III s, and it suggests a role of unusual N i+1 -H···N i hydrogen bonds, in which LanM's unique EF-hand proline residues are engaged, in selective Ln III 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.

Original languageEnglish (US)
Pages (from-to)120-125
Number of pages6
JournalBiochemistry
Volume58
Issue number2
DOIs
StatePublished - Jan 15 2019

    Fingerprint

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this