Crystallization (Comment) | Organism |
---|---|
1.7 A resolution structure of a crystal soaked in CuCl2. A Cu(II) ion is bound to the protein 7.5 A from the T1 copper site in a region rich in methionine residues. The trigonal bipyramidal coordination sphere contains two methionine sulfur atoms, two aspartate carboxylate oxygen atoms, and a water molecule. Asp439 both ligates the labile copper and hydrogen-bonds to His443, which ligates the T1 copper. The type 3 copper atoms of the trinuclear cluster in the structure are bridged by a chloride ion that completes a square planar coordination sphere for the T2 copper atom | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
D360A | mutation in labile copper coordination sphere, inactive | Escherichia coli |
D439A | mutation in labile copper coordination sphere, 3-4fold increase in Km value for Cu2+ | Escherichia coli |
M355L | mutation in labile copper coordination sphere, inactive | Escherichia coli |
M441L | mutation in labile copper coordination sphere. Mutation has affected copper incorporation into the T1 copper site | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.163 | - |
Cu2+ | wild-type, pH 6.5, 23°C | Escherichia coli | |
0.27 | - |
Cu2+ | mutant M441L, pH 6.5, 23°C | Escherichia coli | |
0.59 | - |
Cu2+ | mutant D439A, pH 6.5, 23°C | Escherichia coli | |
1.6 | - |
Cu2+ | mutant D360A, pH 6.5, 23°C | Escherichia coli | |
82 | - |
Cu2+ | mutant M355L, pH 6.5, 23°C | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P36649 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4 Cu2+ + 2 H2O | - |
Escherichia coli | 4 Cu+ + 4 H+ + O2 | - |
? |
Organism | Comment | Expression |
---|---|---|
Escherichia coli | CueO is expressed under conditions of copper stress | up |