Structure-driven development of a biomimetic rare earth artificial metalloprotein.

ABSTRACT: The 2011 discovery of the first rare earth-dependent enzyme in methylotrophic Methylobacterium extorquens AM1 prompted intensive research toward understanding the unique chemistry at play in these systems. This enzyme, an alcohol dehydrogenase (ADH), features a La³⁺ ion closely associated with redox-active coenzyme pyrroloquinoline quinone (PQQ) and is structurally homologous to the Ca²⁺-dependent ADH from the same organism. AM1 also produces a periplasmic PQQ-binding protein, PqqT, which we have now structurally characterized to 1.46-Å resolution by X-ray diffraction. This crystal structure reveals a Lys residue hydrogen-bonded to PQQ at the site analogously occupied by a Lewis acidic cation in ADH. Accordingly, we prepared K₁₄₂A- and K₁₄₂

SUBMITTER: Thompson PJ 

PROVIDER: S-EPMC11331073 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature