Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8 Å resolution

L. Chen, F.S. Mathews, V.L. Davidson, E.G. Huizinga, F.M.D. Vellieux, W.G.J. Hol

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

The three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans (PD-MADH) has been determined at 2.8 Å resolution by the molecular replacement method combined with map averaging procedures, using data collected from an area detector. The structure of methylamine dehydrogenase from Thiobacillus versutus, which contains an 'X-ray' sequence, was used as the starting search model. MADH consists of 2 heavy (H) and 2 light (L) subunits related by a molecular 2- fold axis. The H subunit is folded into seven four-stranded β segments, forming a disk-shaped structure, arranged with pseudo-7-fold symmetry. A 31- residue elongated tail exists at the N-terminus of the H subunit in MADH from T. versutus but is partially digested in this crystal form of MADH from P. denitrificans, leaving the H subunit about 18 residues shorter. Each L subunit contains 127 residues arranged into 10 β-strands connected by turns. The active site of the enzyme is located in the L subunit and is accessible via a hydrophobic channel between the H and L subunits. The redox cofactor of MADH, tryptophan tryptophylquinone is highly unusual. It is formed from two covalently linked tryptophan side chains at positions 57 and 107 of the L subunit, one of which contains an orthoquinone.
Original languageEnglish
Pages (from-to)288-299
Number of pages12
JournalProteins: Structure function and bioinformatics
Volume14
Issue number2
Publication statusPublished - 22 Dec 1992
Externally publishedYes

Keywords

  • amino acid-derived cofactor
  • crystal structure
  • methylamine dehydrogenase
  • molecular replacement
  • oxidoreductase
  • Paracoccus denitrificans
  • pyrroloquinoline quinone
  • quinoprotein
  • tryptophan tryptophylquinone
  • methylamine
  • tryptophan
  • article
  • chemical structure
  • enzyme active site
  • enzyme analysis
  • enzyme structure
  • nonhuman
  • priority journal
  • structure analysis

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