1K2O

Cytochrome P450Cam with Bound BIS(2,2'-BIPYRIDINE)-(5-METHYL-2-2'-BIPYRIDINE)-C2-ADAMANTANE RUTHENIUM (II)

Summary for 1K2O

• Entry DOI: 10.2210/pdb1k2o/pdb
• Related: 1qmq 2cpp
• Descriptor: Cytochrome P450CAM, CACODYLATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• Functional Keywords: p450, monooxygenase, electron transfer, energy transfer, fluorinated aromatics, biphenyl, adamantane, ruthenium channel, substrate-binding, oxidoreductase
• Biological source: Pseudomonas putida
• Cellular location: Cytoplasm (By similarity): P00183
• Total number of polymer chains: 2
• Total formula weight: 99332.66

Authors

Dunn, A.R.,Dmochowski, I.J.,Bilwes, A.M.,Gray, H.B.,Crane, B.R. (deposition date: 2001-09-28, release date: 2001-10-17, Last modification date: 2023-08-16)

Primary citation

Dunn, A.R.,Dmochowski, I.J.,Bilwes, A.M.,Gray, H.B.,Crane, B.R.
Probing the open state of cytochrome P450cam with ruthenium-linker substrates.
Proc.Natl.Acad.Sci.USA, 98:12420-12425, 2001

PubMed Abstract: Cytochromes P450 play key roles in drug metabolism and disease by oxidizing a wide variety of natural and xenobiotic compounds. High-resolution crystal structures of P450cam bound to ruthenium sensitizer-linked substrates reveal an open conformation of the enzyme that allows substrates to access the active center via a 22-A deep channel. Interactions of alkyl and fluorinated biphenyl linkers with the channel demonstrate the importance of exploiting protein dynamics for specific inhibitor design. Large changes in peripheral enzyme structure (F and G helices) couple to conformational changes in active center residues (I helix) implicated in proton pumping and dioxygen activation. Common conformational states among P450cam and homologous enzymes indicate that static and dynamic variability in the F/G helix region allows the 54 human P450s to oxidize thousands of substrates.

PubMed: 11606730
DOI: 10.1073/pnas.221297998

Experimental method

X-RAY DIFFRACTION (1.65 Å)