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Literature summary for 7.2.2.21 extracted from

  • Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Su, X.C.; Miras, R.; Bal, N.; Mintz, E.; Catty, P.; Shokes, J.E.; Scott, R.A.
    Structural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadA (2006), J. Mol. Biol., 356, 638-650.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.2.2.21

Cloned(Commentary)

Cloned (Comment) Organism
N-terminal binding-domain of 71 amino acids carrying a S71A mutation expressed in Escherichia coli M15 Listeria monocytogenes

Crystallization (Commentary)

Crystallization (Comment) Organism
structural analysis of N-terminal enzyme domain, soluble monomeric protein of 71 amino acids, by NMR and X-ray absorption spectroscopy Listeria monocytogenes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + Cd2+/in Escherichia coli active transport of Cd2+ out of the cell to maintain metal homeostasis ADP + phosphate + Cd2+/out
-
 ?
ATP + H2O + Cd2+/in Listeria monocytogenes active transport of Cd2+ out of the cell to maintain metal homeostasis ADP + phosphate + Cd2+/out
-
 ?
ATP + H2O + Zn2+/in Escherichia coli active transport of Cd2+ out of the cell to maintain metal homeostasis ADP + phosphate + Zn2+/out
-
 ?
ATP + H2O + Zn2+/in Listeria monocytogenes active transport of Cd2+ out of the cell to maintain metal homeostasis ADP + phosphate + Zn2+/out
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Listeria monocytogenes Q60048
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminal binding-domain from Escherichia coli Listeria monocytogenes

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + Cd2+[side 1] = ADP + phosphate + Cd2+[side 2] metal binding environment comprises two conserved Cys residues of the metal binding motif and a Glu in loop 5. function of the N-terminus in the metal specificity of the enzyme Listeria monocytogenes
a
ATP + H2O + Cd2+[side 1] = ADP + phosphate + Cd2+[side 2] Cys14, Cys17 and Glu61 involved in metal binding Listeria monocytogenes
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Cd2+/in active transport of Cd2+ out of the cell to maintain metal homeostasis Escherichia coli ADP + phosphate + Cd2+/out
-
 ?
ATP + H2O + Cd2+/in active transport of Cd2+ out of the cell to maintain metal homeostasis Listeria monocytogenes ADP + phosphate + Cd2+/out
-
 ?
ATP + H2O + Zn2+/in active transport of Cd2+ out of the cell to maintain metal homeostasis Escherichia coli ADP + phosphate + Zn2+/out
-
 ?
ATP + H2O + Zn2+/in active transport of Cd2+ out of the cell to maintain metal homeostasis Listeria monocytogenes ADP + phosphate + Zn2+/out
-
 ?

Subunits

Subunits Comment Organism
dimer N-terminal binding-domain with bound metal ion Listeria monocytogenes
monomer N-terminal binding-domain without bound metal ion Listeria monocytogenes

Synonyms

Synonyms Comment Organism
CadA
-
 Listeria monocytogenes
NTKII N-terminal binding-domain of 71 amino acids carrying a S71A mutation Listeria monocytogenes
ZntA
-
 Escherichia coli