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Literature summary for 7.6.2.8 extracted from

  • Korkhov, V.M.; Mireku, S.A.; Veprintsev, D.B.; Locher, K.P.
    Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F (2014), Nat. Struct. Mol. Biol., 21, 1097-1099.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant E159Q/N162C in complex with adenylyl imidodiphosphate, sitting drop vapor diffusion method, using 100 mM ADA buffer, pH 6.9, 1.2 M NaCl, and 14-18% (w/v) PEG 2000 MME Escherichia coli

Protein Variants

Protein Variants Comment Organism
E159Q/N162C the mutant shows dramatically reduced ATPase activity Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P06609
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
BtuCD
-
Escherichia coli