Literature summary extracted from
Lee, Y.T.; Wilson, R.F.; Rupniewski, I.; Goodin, D.B.
P450cam visits an open conformation in the absence of substrate (2010), Biochemistry, 49, 3412-3419.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.14.15.1 |
overexpression of P450cam mutant C334A in Escherichia coli strain BL21(DE3) |
Pseudomonas putida |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.14.15.1 |
camphor-free or camphor-bound P450cam mutant C334A in the absence of substrate and at high and low K+ concentration, protein in 50 mM Tris, pH 7.4, with or without 2-4 mM camphor, mixed with crystallization solution containing 50 mM Tris, pH 7.4, and 12-22% PEG 8000 with and without 200 mM K+, sitting drop vapour diffusion method, 6°C, X-ray diffraction structure determination and analysis at 1.50-1.79 A resolution |
Pseudomonas putida |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.14.15.1 |
C334A |
the mutation of P450cam increases the protein stability compared to the wild-type enzyme |
Pseudomonas putida |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.14.15.1 |
Pseudomonas putida |
P00183 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.14.15.1 |
recombinant P450cam mutant C334A from Escherichia coli strain BL21(DE3) by anion exchange chromatography and gel filtration |
Pseudomonas putida |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.14.15.1 |
More |
the camphor-free structure is in an open conformation characterized by a water-filled channel created by the retraction of the F and G helices, disorder of the B' helix, and loss of the K+ binding. site. Presence of K+ alone does not alter the open conformation, while camphor alone is sufficient for closure of the channel |
Pseudomonas putida |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.14.15.1 |
P450cam |
- |
Pseudomonas putida |