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Literature summary for 7.2.2.14 extracted from

  • Wang, S.Z.; Chen, Y.; Sun, Z.H.; Zhou, Q.; Sui, S.F.
    Escherichia coli CorA periplasmic domain functions as a homotetramer to bind substrate (2006), J. Biol. Chem., 281, 26813-26820.
    View publication on PubMed
Search for more literature for 7.2.2.14

Crystallization (Commentary)

Crystallization (Comment) Organism
single particle electron microscopy of recombinant periplasmic domain, enzyme is a pyramid-like homotetramer with a central cavity Escherichia coli

Protein Variants

Protein Variants Comment Organism
C191A elimination of the only Cys residue of enzyme, mutant forms a tetramer like wild-type Escherichia coli
additional information purified recombinant periplasmic domain of enzyme retains its substrate binding ability as native enzyme Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
132000
-
 gel filtration, recombinant periplasmic domain Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 recombinant periplasmic domain, glutathione S-transferase fusion protein
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information disulfide bonds do not participate in tetramer formation Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
recombinant periplasmic domain, glutathione S-transferase fusion protein Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Co2+/in apparent dissociation constant: wild-type, 0.0298 mM, recombinant periplasmic domain, 0.0236 mM Escherichia coli ADP + phosphate + Co2+/out
-
 ?
ATP + H2O + Mg2+/in apparent dissociation constant: wild-type, 0.0184 mM, recombinant periplasmic domain, 0.0309 mM9 Escherichia coli ADP + phosphate + Mg2+/out
-
 ?
ATP + H2O + Ni2+/in apparent dissociation constant: wild-type, 0.201 mM, recombinant periplasmic domain, 0.106 mM Escherichia coli ADP + phosphate + Ni2+/out
-
 ?

Subunits

Subunits Comment Organism
homotetramer SDS-PAGE Escherichia coli