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Literature summary for 1.14.99.39 extracted from

  • Lawton, T.J.; Ham, J.; Sun, T.; Rosenzweig, A.C.
    Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily (2014), Proteins, 82, 2263-2267 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.99.39

Cloned(Commentary)

Cloned (Comment) Organism
gene amoB, amino acids 31-186, sequence determination and analysis, recombinant expression as C-terminally Strep-tagged protein in Escherichia coli strain Rosetta-2 (DE3) using pASK-IBA2 vector Candidatus Nitrosocaldus yellowstonensis

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant Ny_amoB, amino acids 31-186, sitting drop vapor diffusion method, mixing 0.001 ml of 5 mg/ml protein solution with 0.0035 ml of well solution containing 1 M (NH4)2SO4, 100 mM sodium formate, pH 4.0, and 2% PEG 8000, football shaped crystals appear within 2-3 days, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling Candidatus Nitrosocaldus yellowstonensis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound Candidatus Nitrosocaldus yellowstonensis 16020
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Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ an N-terminal copper binding site Candidatus Nitrosocaldus yellowstonensis

Organism

Organism UniProt Comment Textmining
Candidatus Nitrosocaldus yellowstonensis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally Strep-tagged protein, comprising amino acids 31-186, from Escherichia coli strain Rosetta-2 (DE3) by affinity chromatography, ultrafiltration, and gel filtration Candidatus Nitrosocaldus yellowstonensis

Synonyms

Synonyms Comment Organism
ammonia monooxygenase
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 Candidatus Nitrosocaldus yellowstonensis
AMO
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 Candidatus Nitrosocaldus yellowstonensis
AmoB
-
 Candidatus Nitrosocaldus yellowstonensis
Ny_amoB
-
 Candidatus Nitrosocaldus yellowstonensis

General Information

General Information Comment Organism
evolution the enzyme belongs to the ammonia monooxygenase (AMO)/particulate methane monooxygenase (pMMO) superfamily, copper membrane-associated monooxygenases (CuMOs), which is a diverse group of membrane-bound enzymes. The Ny_amoB structure reveals that the fold of the N-terminal domain of the B subunit in the AMO/pMMO superfamily is very well conserved as is the presence of an N-terminal copper binding site Candidatus Nitrosocaldus yellowstonensis
additional information the pMMO active site is believed to reside in the soluble N-terminal region of the pmoB subunit. Modeling and structure comparisons of the N-terminal domain of the B subunit in the AMO/pMMO superfamily Candidatus Nitrosocaldus yellowstonensis
physiological function enzyme AMO converts ammonia to hydroxylamine in nitrifiers Candidatus Nitrosocaldus yellowstonensis