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Literature summary for 7.3.2.1 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 PubMed
Search for more literature for 7.3.2.1

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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)

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

Organism

Organism UniProt Comment Textmining
Clostridium perfringens A0A0H2YSI2
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

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