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Literature summary for 7.6.2.8 extracted from

  • Kandt, C.; Xu, Z.; Tieleman, D.P.
    Opening and closing motions in the periplasmic vitamin B12 binding protein BtuF (2006), Biochemistry, 45, 13284-13292.
    View publication on PubMed
Search for more literature for 7.6.2.8

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 strain K12
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 principal motions and conformational changes of apo and holo forms studied, closed conformation for the ligand-bound state identified, empty form shown to fluctuate between open and closed conformations, simulation system and force field parameters described, elastic network normal-mode analysis performed, conformational changes summarized, domain motions indicated, link to previous simulations and biological implications discussed 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 480 ns multicopy molecular dynamics simulations performed, dynamics of apo and holo forms of the protein analyzed, opening and closing motions more pronounced in the apo form Escherichia coli ADP + phosphate + vitamin B12/in
-
 ?

Synonyms

Synonyms Comment Organism
BtuF
-
 Escherichia coli