Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: High resolution structure and functional properties

Sam Yong Park, Kazuhide Yamane, Shin Ichi Adachi, Yoshitsugu Shiro, Kara E. Weiss, Shelley A. Maves, Stephen G. Sligar

Research output: Contribution to journalArticlepeer-review

Abstract

Crystal structures of a thermostable cytochrome P450 (CYP119) and a site-directed mutant, (Phe24Leu), from the acidothermophilic archaea Sulfolobus solfataricus were determined at 1.5-2.0 Å resolution. We identify important crystallographic waters in the ferric heme pocket, observe protein conformational changes upon inhibitor binding, and detect a unique distribution of surface charge not found in other P450s. An analysis of factors contributing to thermostability of CYP119 of these high resolution structures shows an apparent increase in clustering of aromatic residues and optimum stacking. The contribution of aromatic stacking was investigated further with the mutant crystal structure and differential scanning calorimetry.

Original languageEnglish (US)
Pages (from-to)491-501
Number of pages11
JournalJournal of Inorganic Biochemistry
Volume91
Issue number4
DOIs
StatePublished - Sep 20 2002

Keywords

  • Crystal structure
  • Cytochrome P450
  • Thermophilic

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

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