1IO8

Thermophilic cytochrome P450 (CYP119) from sulfolobus solfataricus: High resolution structural origin of its thermostability and functional properties

Summary for 1IO8

• Entry DOI: 10.2210/pdb1io8/pdb
• Related: 1IO7 1IO9
• Descriptor: CYTOCHROME P450 CYP119, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: thermophilic, cytochromo p450, riken structural genomics/proteomics initiative, rsgi, structural genomics, oxidoreductase, nppsfa, national project on protein structural and functional analyses
• Biological source: Sulfolobus solfataricus
• Cellular location: Cytoplasm (Probable): Q55080
• Total number of polymer chains: 2
• Total formula weight: 87013.00

Authors

Park, S.-Y.,Yamane, K.,Adachi, S.,Shiro, Y.,Sligar, S.G.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2001-02-08, release date: 2001-03-07, Last modification date: 2024-04-03)

Primary citation

Park, S.Y.,Yamane, K.,Adachi, S.,Shiro, Y.,Weiss, K.E.,Maves, S.A.,Sligar, S.G.
Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: high resolution structure and functional properties
J.Inorg.Biochem., 91:491-501, 2002

PubMed 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 A 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.

PubMed: 12237217
DOI: 10.1107/S0907444900008234

Experimental method

X-RAY DIFFRACTION (2 Å)