3FWF

Ferric camphor bound cytochrome P450cam containing a Selenocysteine as the 5th heme ligand, monoclinic crystal form

Summary for 3FWF

• Entry DOI: 10.2210/pdb3fwf/pdb
• Related: 1dz4
• Descriptor: Camphor 5-monooxygenase, PROTOPORPHYRIN IX CONTAINING FE, CAMPHOR, ... (5 entities in total)
• Functional Keywords: selenocysteine, hemoprotein, cytochrome p450, cytochrome, heme, iron, metal-binding, monooxygenase, oxidoreductase
• Biological source: Pseudomonas putida
• Cellular location: Cytoplasm : P00183
• Total number of polymer chains: 2
• Total formula weight: 92981.45

Authors

Schlichting, I.,Von Koenig, K.,Aldag, C.,Hilvert, D. (deposition date: 2009-01-18, release date: 2009-03-03, Last modification date: 2024-02-21)

Primary citation

Aldag, C.,Gromov, I.A.,Garcia-Rubio, I.,von Koenig, K.,Schlichting, I.,Jaun, B.,Hilvert, D.
Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine.
Proc.Natl.Acad.Sci.USA, 106:5481-5486, 2009

PubMed Abstract: The unique monooxygenase activity of cytochrome P450cam has been attributed to coordination of a cysteine thiolate to the heme cofactor. To investigate this interaction, we replaced cysteine with the more electron-donating selenocysteine. Good yields of the selenoenzyme were obtained by bacterial expression of an engineered gene containing the requisite UGA codon for selenocysteine and a simplified yet functional selenocysteine insertion sequence (SECIS). The sulfur-to-selenium substitution subtly modulates the structural, electronic, and catalytic properties of the enzyme. Catalytic activity decreases only 2-fold, whereas substrate oxidation becomes partially uncoupled from electron transfer, implying a more complex role for the axial ligand than generally assumed.

PubMed: 19293375
DOI: 10.1073/pnas.0810503106

Experimental method

X-RAY DIFFRACTION (1.83 Å)