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Literature summary extracted from

  • Gonzalez, D.; Richez, M.; Bergonzi, C.; Chabriere, E.; Elias, M.
    Crystal structure of the phosphate-binding protein (PBP-1) of an ABC-type phosphate transporter from Clostridium perfringens (2014), Sci. Rep., 4, 6636.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.3.2.1 expressed in Escherichia coli BL21(DE3)-pGro7/GroEL cells Clostridium perfringens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.3.2.1 in complex with phosphate, sitting drop vapor diffusion method, using 0.1 M sodium acetate, 0.2 M zinc acetate pH 4.5, and 10% (w/v) PEG 3000 Clostridium perfringens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.3.2.1 ATP + H2O + phosphate/out Clostridium perfringens
-
 ADP + phosphate + phosphate/in
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.3.2.1 Clostridium perfringens A0A0H2YSI2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.3.2.1 HisTrap nickel affinity column chromatography and Superdex 75 gel filtration Clostridium perfringens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.3.2.1 ATP + H2O + arsenate/out the enzyme has about 150fold lower affinity for arsenate compared to phosphate Clostridium perfringens ADP + phosphate + arsenate/in
-
 ?
7.3.2.1 ATP + H2O + phosphate/out
-
 Clostridium perfringens ADP + phosphate + phosphate/in
-
 ?

Synonyms

EC Number Synonyms Comment Organism
7.3.2.1 high affinity phosphate-binding protein
-
 Clostridium perfringens
7.3.2.1 PBP-1
-
 Clostridium perfringens