1F4U

THERMOPHILIC P450: CYP119 FROM SULFOLOBUS SOLFACTARICUS

Summary for 1F4U

• Entry DOI: 10.2210/pdb1f4u/pdb
• Related: 1F4T
• Descriptor: CYTOCHROME P450 119, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: p450 fold, oxidoreductase
• Biological source: Sulfolobus solfataricus
• Cellular location: Cytoplasm : Q55080
• Total number of polymer chains: 2
• Total formula weight: 87411.32

Authors

Yano, J.K.,Koo, L.S.,Schuller, D.J.,Li, H.,Ortiz de Montellano, P.R.,Poulos, T.L. (deposition date: 2000-06-09, release date: 2000-10-23, Last modification date: 2024-02-07)

Primary citation

Yano, J.K.,Koo, L.S.,Schuller, D.J.,Li, H.,Ortiz de Montellano, P.R.,Poulos, T.L.
Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus.
J.Biol.Chem., 275:31086-31092, 2000

PubMed Abstract: The structure of the first P450 identified in Archaea, CYP119 from Sulfolobus solfataricus, has been solved in two different crystal forms that differ by the ligand (imidazole or 4-phenylimidazole) coordinated to the heme iron. A comparison of the two structures reveals an unprecedented rearrangement of the active site to adapt to the different size and shape of ligands bound to the heme iron. These changes involve unraveling of the F helix C-terminal segment to extend a loop structure connecting the F and G helices, allowing the longer loop to dip down into the active site and interact with the smaller imidazole ligand. A comparison of CYP119 with P450cam and P450eryF indicates an extensive clustering of aromatic residues may provide the structural basis for the enhanced thermal stability of CYP119. An additional feature of the 4-phenylimidazole-bound structure is a zinc ion tetrahedrally bound by symmetry-related His and Glu residues.

PubMed: 10859321
DOI: 10.1074/jbc.M004281200

Experimental method

X-RAY DIFFRACTION (2.69 Å)