Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily

Thomas J. Lawton, Jungwha Ham, Tianlin Sun, Amy C. Rosenzweig*

*Corresponding author for this work

Research output: Contribution to journalArticle

30 Scopus citations

Abstract

The ammonia monooxygenase (AMO)/particulate methane monooxygenase (pMMO) superfamily is a diverse group of membrane-bound enzymes of which only pMMO has been characterized on the molecular level. The pMMO active site is believed to reside in the soluble N-terminal region of the pmoB subunit. To understand the degree of structural conservation within this superfamily, the crystal structure of the corresponding domain of an archaeal amoB subunit from Nitrosocaldus yellowstonii has been determined to 1.8 Å resolution. The structure reveals a remarkable conservation of overall fold and copper binding site location as well as several notable differences that may have implications for function and stability.

Original languageEnglish (US)
Pages (from-to)2263-2267
Number of pages5
JournalProteins: Structure, Function and Bioinformatics
Volume82
Issue number9
DOIs
StatePublished - Sep 2014

Keywords

  • AMO
  • AmoB
  • Copper
  • Crystal structure
  • Cupredoxin
  • Hydrocarbon monooxygenase
  • Methanotroph
  • PMMO

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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