Crystal structure and refinement of cytochrome P450terp at 2·3 Å resolution

Charles A. Hasemann, K. G. Ravichandran, Julian A. Peterson, Johann Deisenhofer

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380 Scopus citations


Cytochrome P450terp is a class I (mitochondrial/bacterial) P450 that catalyzes the hydroxylation of α-terpineol as part of the catabolic assimilation of this compound by a pseudomonad species. Crystals grown from the purified protein have the symmetry of space group P6122, and cell dimensions a = b = 69·4 A ̊, c = 456·6 A ̊, α = β = 90°, γ = 120°. Diffraction data were collected at the Cornell High Energy Synchrotron Source, and the structure of P450terp was solved by a combination of molecular replacement and multiple isomorphous replacement techniques. A model of P450terp was built and refined against native data, to an R-factor of 18·9% for data with I ≥ σ(I) between 6·0 Å and 2·3 Å resolution. This model contains 412 of the 428 P450terp amino acid residues; the loop between helices F and G is disordered in the crystal. While the overall fold of P450terp is very similar to that of P450cam, only three-quarters of the C positions can be superimposed, to a root-mean-square deviation of only 1·87 Å. The mode of substrate binding by P450terp can be predicted, and probable substrate contact residues identified. The heme environment and side-chain positions in the adjacent I-helix suggest possible modes of proton delivery in the catalytic cycle of the enzyme.

Original languageEnglish (US)
Pages (from-to)1169-1185
Number of pages17
JournalJournal of Molecular Biology
Issue number4
StatePublished - Mar 4 1994


  • crystal structure
  • cytochrome P450
  • hemoprotein
  • molecular replacement
  • synchrotron radiation

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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