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Literature summary for 7.6.2.8 extracted from

  • Priess, M.; Schaefer, L.V.
    Release of entropic spring reveals conformational coupling mechanism in the ABC transporter BtuCD-F (2016), Biophys. J., 110, 2407-2418 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.6.2.8

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant wild-type BtuCD-F, apo-BtuCD-F, and BtuCD-F mutant E159Q/N162C, X-ray diffraction structure determination and analysis Escherichia coli

Protein Variants

Protein Variants Comment Organism
E159Q/N162C site-directed mutagenesis, a disulfide mutant, analysis of the crystal structure of the mutant with bound ATP Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
inner membrane
-
 Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] Escherichia coli
-
 ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P06609 AND P06611 AND P37028 genes btuC, btuD, and btuF encoding for vitamin B12 import system permease protein BtuC, vitamin B12 import ATP-binding protein BtuD, and vitamin B12-binding protein BtuF
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1]
-
 Escherichia coli ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
-
 ?

Subunits

Subunits Comment Organism
homodimer
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
BtuCD-F
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP binding structure and conformational coupling, molecular dynamics simulations using BtuCD-F is embedded in a solvated phosphatidylcholine bilayer, configurational entropy, pairwise residue-residue forces in BtuCD-F are analyzed through force distribution analysis, overview Escherichia coli

General Information

General Information Comment Organism
additional information conformational coupling, molecular dynamics simulations using BtuCD-F is embedded in a solvated phosphatidylcholine bilayer, configurational entropy, pairwise residue-residue forces in BtuCD-F are analyzed through force distribution analysis, overview Escherichia coli
physiological function the ABC transporter BtuCD-F imports vitamin B12 across the inner membrane of Escherichia coli. Substrate translocation by ATP-binding cassette (ABC) transporters involves coupling of ATP binding and hydrolysis in the nucleotide-binding domains (NBDs) to conformational changes in the transmembrane domains Escherichia coli