6MI5

NMR solution structure of lanmodulin (LanM) complexed with yttrium(III) ions

6MI5 の概要

• エントリーDOI: 10.2210/pdb6mi5/pdb
• NMR情報: BMRB: 30515
• 分子名称: Lanmodulin, YTTRIUM (III) ION (2 entities in total)
• 機能のキーワード: lanthanide, ef-hand, methylotroph, periplasm, metal binding protein
• 由来する生物種: Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12796.49

構造登録者

Cook, E.C.,Featherson, E.R.,Showalter, S.A.,Cotruvo Jr., J.A. (登録日: 2018-09-19, 公開日: 2018-11-07, 最終更新日: 2024-05-01)

主引用文献

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

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: 30352145
DOI: 10.1021/acs.biochem.8b01019

実験手法

SOLUTION NMR