4O65 : Crystal structure of the cupredoxin domain of amoB from Nitrosocaldus yellowstonii

  • T. J. Lawton (Contributor)
  • Jungwha Ham (Contributor)
  • Tianlin Sun (Contributor)
  • Amy C Rosenzweig (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Release Date:2014-04-02
Deposition Date:2013-12-20
Revision Date:2014-09-03#2014-11-12
Molecular Weight:18412.09
Macromolecule Type:Protein
Residue Count:166
Atom Site Count:1199

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.
Date made available2014

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