Secondary Structure Prediction of 52 Membrane-Bound Cytochromes P450 Shows a Strong Structural Similarity to P450cam

David Nelson, Henry W. Strobel

Research output: Contribution to journalArticle

131 Citations (Scopus)

Abstract

The secondary structure of 52 aligned cytochrome P450 sequences, all of which are membrane bound, is predicted and collectively compared with the crystal structure of the soluble cytochrome P450cam. Ten of 13 helical regions, 6 of 7 β-pair regions, and β-structure corresponding to a known γ-bulge near the active site of P450cam are predicted to exist in the membrane-bound P450s. Three turns associated with β-structure in the soluble enzyme are also predicted for the membrane-bound forms. A strong structural similarity is evident between membrane P450s and the soluble P450cam. Consequently, a multitransmembrane structure involving much of P450 seems highly unlikely. A structure with two N-terminal transmembrane segments is compatible with these observations.

Original languageEnglish (US)
Pages (from-to)656-660
Number of pages5
JournalBiochemistry
Volume28
Issue number2
DOIs
StatePublished - Jan 1 1989
Externally publishedYes

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Camphor 5-Monooxygenase
Cytochrome P-450 Enzyme System
Membranes
Cytochromes
Catalytic Domain
Crystal structure
Enzymes

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Secondary Structure Prediction of 52 Membrane-Bound Cytochromes P450 Shows a Strong Structural Similarity to P450cam. / Nelson, David; Strobel, Henry W.

In: Biochemistry, Vol. 28, No. 2, 01.01.1989, p. 656-660.

Research output: Contribution to journalArticle

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