English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons137577

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

/persons/resource/persons137633

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

/persons/resource/persons137648

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

External Resource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
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: http://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.