How an Enzyme Binds the C1 Carrier Tetrahydromethanopterin. Structure of the 
Tetrahydromethanopterin-Dependent Formaldehyde-Activating Enzyme (Fae) from 
Methylobacterium extorquens AM1

Acharya, Priyamvada; Gornrich, Meike; Hagemeier, Christoph; Vorholt, Julia A.; Thauer, Rudolf K.; Ermler, Ulrich

doi:10.1074/jbc.M412320200

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How an Enzyme Binds the C₁ Carrier Tetrahydromethanopterin. Structure of the Tetrahydromethanopterin-Dependent Formaldehyde-Activating Enzyme (Fae) from Methylobacterium extorquens AM1

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Acharya, Priyamvada
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Max-Planck-Institut für terrestrische Mikrobiologie, 35043 Marburg, Germany;

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Demmer, Ulrike
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Ermler, Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Acharya, P., Gornrich, M., Hagemeier, C., Vorholt, J. A., Thauer, R. K., & Ermler, U. (2005). How an Enzyme Binds the C₁ Carrier Tetrahydromethanopterin. Structure of the Tetrahydromethanopterin-Dependent Formaldehyde-Activating Enzyme (Fae) from Methylobacterium extorquens AM1. The Journal of Biological Chemistry, 280(14), 13712-13719. doi:10.1074/jbc.M412320200.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DA3B-7

Abstract

Tetrahydromethanopterin (H₄ MPT) is a tetrahydrofolate analogue involved as a C₁ carrier in the metabolism of various groups of microorganisms. How H₄MPT is bound to the respective C₁ unit converting enzymes remained elusive. We describe here the structure of the homopentameric formaldehyde-activating enzyme (Fae) from Methylobacterium extorquens AM1 established at 2.0 angstrom without and at 1.9 angstrom with methylene-H₄MPT bound. Methylene-H₄MPT is bound in an "S"-shaped conformation into the cleft formed between two adjacent subunits. Coenzyme binding is accompanied by side chain rearrangements up to 5 angstrom and leads to a rigidification of the C-terminal arm, a formation of a new hydrophobic cluster, and an inversion of the amide side chain of Gln⁸⁸. Methylene-H₄MPT in Fae shows a characteristic kink between the tetrahydropyrazine and the imidazolidine rings of 70 degrees that is more pronounced than that reported for free methylene-H₄MPT in solution (50 degrees). Fae is an essential enzyme for energy metabolism and formaldehyde detoxification of this bacterium and catalyzes the formation of methylene-H₄MPT from H₄MPT and formaldehyde. The molecular mechanism ofthis reaction involving His²² as acid catalyst is discussed.