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Literature summary for 7.6.2.8 extracted from

  • Hvorup, R.N.; Goetz, B.A.; Niederer, M.; Hollenstein, K.; Perozo, E.; Locher, K.P.
    Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF (2007), Science, 317, 1387-1390.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
BtuCD-F complex analyzed at a resolution of 2.6 A, substantial conformational changes observed as compared with previously reported structures of BtuCD and BtuF Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
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 P06611 encoded by btuD gene
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
crystal structure of BtuCD-F complex presented, displacement of vitamin B12 from binding pocket shown, subunits of transmembrane BtuC protein shown to have two distinct conformations, translocation pathway shown to be closed to both sides of the membrane, electron paramagnetic resonance spectra of spin-labeled cysteine mutants shown to be consistent with the conformation of BtuCD-F observed in the crystal structure, structure of BtuCD-F discussed as a posttranslocation intermediate 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
-
?
ATP + H2O + vitamin B12/out crystal structure of BtuCD-F complex determined, BtuF protein shown to be bound to the periplasmic face of BtuCD Escherichia coli ADP + phosphate + vitamin B12/in
-
?