Structures of the methyltransferase component of Desulfitobacterium hafniense DCB-2 O-demethylase shed light on methyltetrahydrofolate formation

Acta Crystallographica. Section D, Biological Crystallography
Hanno SjutsDavid Leys

Abstract

O-Demethylation by acetogenic or organohalide-respiring bacteria leads to the formation of methyltetrahydrofolate from aromatic methyl ethers. O-Demethylases, which are cobalamin-dependent, three-component enzyme systems, catalyse methyl-group transfers from aromatic methyl ethers to tetrahydrofolate via methylcobalamin intermediates. In this study, crystal structures of the tetrahydrofolate-binding methyltransferase module from a Desulfitobacterium hafniense DCB-2 O-demethylase were determined both in complex with tetrahydrofolate and the product methyltetrahydrofolate. While these structures are similar to previously determined methyltransferase structures, the position of key active-site residues is subtly altered. A strictly conserved Asn is displaced to establish a putative proton-transfer network between the substrate N5 and solvent. It is proposed that this supports the efficient catalysis of methyltetrahydrofolate formation, which is necessary for efficient O-demethylation.

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Jul 31, 2013·Acta Crystallographica. Section D, Biological Crystallography·Hanno SjutsDavid Leys

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Citations

Dec 25, 2016·Journal of Structural and Functional Genomics·Clara Shionyu-MitsuyamaTsuyoshi Shirai
Sep 14, 2019·Chembiochem : a European Journal of Chemical Biology·Thomas Badmann, Michael Groll
Aug 3, 2021·Frontiers in Microbiology·Veronika KivensonDavid L Valentine

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