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Literature summary extracted from

  • Korkhov, V.M.; Mireku, S.A.; Locher, K.P.
    Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F (2012), Nature, 490, 367-372.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.6.2.8 in complex with beta-gamma-imidoadenosine 5'-triphosphate, sitting drop vapor diffusion method, using 20-30% (w/v) PEG 400, 100 mM N-(2-acetamido)-iminodiacetic acid, pH 6.8, 100 mM sodium potassium citrate Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
7.6.2.8 E159Q/N162C the mutant is unable to transport substrate despite a very low residual ATP hydrolysis rate Escherichia coli
7.6.2.8 L85C the mutant shows a 6.5fold reduction in ATPase activity compared to the wild type enzyme Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.6.2.8 ATP + H2O + vitamin B12/out Escherichia coli
-
 ADP + phosphate + vitamin B12/in
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.6.2.8 Escherichia coli P06609
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.6.2.8 purified in 0.1% n-dodecyl-N,N-dimethylamine-N-oxide Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.6.2.8 ATP + H2O + vitamin B12/out
-
 Escherichia coli ADP + phosphate + vitamin B12/in
-
 ?

Synonyms

EC Number Synonyms Comment Organism
7.6.2.8 BtuCD-F
-
 Escherichia coli
7.6.2.8 vitamin B12 transporter
-
 Escherichia coli