Structural highlights
4jx1 is a 8 chain structure with sequence from "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Ligands: | 1N0, CA, CAH, CAM, FES, HEM |
| Related: | 4jws, 4jwu |
| Gene: | camC, cyp101 ("Bacillus fluorescens putidus" Flugge 1886), camB ("Bacillus fluorescens putidus" Flugge 1886) |
| Activity: | Camphor 5-monooxygenase, with EC number 1.14.15.1 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[CPXA_PSEPU] Involved in a camphor oxidation system. [PUTX_PSEPU] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.
Publication Abstract from PubMed
Cytochromes P450 catalyze a variety of monooxygenase reactions that require electron transfer from redox partners. Although the structure of many P450s and a small handful of redox partners are known, there is very little structural information available on redox complexes, thus leaving a gap in our understanding on the control of P450-redox partner interactions. We have solved the crystal structure of oxidized and reduced P450cam complexed with its redox partner, putidaredoxin (Pdx), to 2.2 and 2.09 angstroms, respectively. It was anticipated that Pdx would favor closed substrate-bound P450cam, which differs substantially from the open conformer, but instead we found that Pdx favors the open state. These new structures indicate that the effector role of Pdx is to shift P450cam toward the open conformation, which enables the establishment of a water-mediated H-bonded network, which is required for proton-coupled electron transfer.
Structural basis for effector control and redox partner recognition in cytochrome P450.,Tripathi S, Li H, Poulos TL Science. 2013 Jun 7;340(6137):1227-30. doi: 10.1126/science.1235797. PMID:23744947[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tripathi S, Li H, Poulos TL. Structural basis for effector control and redox partner recognition in cytochrome P450. Science. 2013 Jun 7;340(6137):1227-30. doi: 10.1126/science.1235797. PMID:23744947 doi:10.1126/science.1235797
