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  Structure of methylene-tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1

Ermler, U., Hagemeier, C. H., Roth, A., Demmer, U., Grabarse, W., Warkentin, E., et al. (2002). Structure of methylene-tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1. Structure, 10(8), 1127-1137. doi:10.1016/S0969-2126(02)00802-X.

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 Creators:
Ermler, Ulrich1, Author                 
Hagemeier, Christoph H.2, Author
Roth, Annette1, Author           
Demmer, Ulrike1, Author           
Grabarse, Wolfgang1, Author           
Warkentin, Eberhard1, Author           
Vorhott, Julia A.2, 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              

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Free keywords: Electron-density maps; Crystal-structure; Methylotrophic bacteria; Methanopyrus-kandleri; Methanogenic archaea; Dependent enzymes; Protein; Cyclohydrolase; Binding; Dehydrogenase/cyclohydrolase
 Abstract: NADP-dependent methylene-H4MPT dehydrogenase, MtdA, from Methylobacterium extorquens AM1 catalyzes the dehydrogenation of methylene-tetrahydro-methanopterin and methylene-tetrahydrofolate with NADP(+) as cosubstrate. The X-ray structure of MtdA with and without NADP bound was established at 1.9 Angstrom resolution. The enzyme is present as a homotrimer. The alpha,beta fold of the monomer is related to that of methylene-H4F dehydrogenases, suggesting a common evolutionary origin. The position of the active site is located within a large crevice built up by the two domains of one subunit and one domain of a second subunit. Methylene-H4MPT could be modeled into the cleft, and crucial active site residues such as Phe18, Lys256, His260, and Thr102 were identified. The molecular basis of the different substrate specificities and different catalytic demands of MtdA compared to methylene-H4F dehydrogenases are discussed. [References: 47]

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Language(s): eng - English
 Dates: 2002-05-102002-01-282002-05-132002-08-132002-08
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0969-2126(02)00802-X
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Title: Structure
  Other : Structure
Source Genre: Journal
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Publ. Info: London : Cell Press
Pages: - Volume / Issue: 10 (8) Sequence Number: - Start / End Page: 1127 - 1137 Identifier: ISSN: 0969-2126
CoNE: https://pure.mpg.de/cone/journals/resource/954927002244_1