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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

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.

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 Creators:
Acharya, Priyamvada1, 2, Author           
Gornrich, Meike2, Author
Hagemeier, Christoph2, Author
Demmer, Ulrike1, Contributor           
Vorholt, Julia A.3, Author
Thauer, Rudolf K.2, Author
Ermler, Ulrich1, Author           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Max-Planck-Institut für terrestrische Mikrobiologie, 35043 Marburg, Germany, ou_persistent22              
3Institut National de La Recherche Agronomique/CNRS, BP27 Chemin de Borde Rouge, F-31326 Castanet-Tolosan, France, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2004-12-072004-11-042021-01-042005-04-08
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.M412320200
PMID: 15632161
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 280 (14) Sequence Number: - Start / End Page: 13712 - 13719 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1