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Literature summary for 7.6.2.8 extracted from

  • Schmitt, L.
    Vitamin B12 import is all about timing (2018), Nat. Chem. Biol., 14, 640-641 .
    View publication on PubMed
Search for more literature for 7.6.2.8

Localization

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

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
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 ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
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 ?

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
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Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] = ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] transport mechanism, model building showing the substantial conformational changes to catalyze the translocation of their substrates across biological membranes, overview. The transport cycle of BtuCD-F can be divided into a futile cycle in the absence of the substrate-binding protein and a productive cycle in the presence of vitamin B12-loaded substrate-binding protein Escherichia coli
a

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]
-
 ?

Synonyms

Synonyms Comment Organism
BtuCD-F
-
 Escherichia coli
vitamin B12 import system
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
additional information ABC importers follow the two-site access model3, in which ATP binding and hydrolysis switch the accessibility of the transmembrane domain for the substrate from an inward facing (accessible from the cytoplasm) to an outward-facing (accessible from the extracellular site) conformation, conformational changes by single-molecule FRET measurements combined with molecular dynamics simulations, two different transport cycles are analyzed Escherichia coli
physiological function the ATP-binding cassette (ABC) importer family catalyzse the uptake of nutrients, vitamins and trace elements. Membrane transport proteins generally are inherently flexible and undergo substantial conformational changes to catalyze the translocation of their substrates across biological membranes. The vitamin B12 import system BtuCD-F from Escherichia coli shows the conformational dynamics during the transport cycle Escherichia coli