4JWU

Crystal structure of Cytochrome P450cam-putidaredoxin complex

Summary for 4JWU

• Entry DOI: 10.2210/pdb4jwu/pdb
• Related: 4JWS 4JX1
• Descriptor: Camphor 5-monooxygenase, Putidaredoxin, PROTOPORPHYRIN IX CONTAINING FE, ... (7 entities in total)
• Functional Keywords: p450cam-pdx complex, redox partners, oxidoreductase-electron transport complex, oxidoreductase/electron transport
• Biological source: Pseudomonas putida; More
• Cellular location: Cytoplasm : P00183
• Total number of polymer chains: 4
• Total formula weight: 119862.47

Authors

Tripathi, S.M.,Li, H.,Poulos, T.L. (deposition date: 2013-03-27, release date: 2013-06-19, Last modification date: 2024-10-16)

Primary citation

Tripathi, S.,Li, H.,Poulos, T.L.
Structural basis for effector control and redox partner recognition in cytochrome P450.
Science, 340:1227-1230, 2013

PubMed Abstract: 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.

PubMed: 23744947
DOI: 10.1126/science.1235797

Experimental method

X-RAY DIFFRACTION (2.2 Å)