PDBsum entry 1f4t

Oxidoreductase

PDB id: 1f4t

Contents

Protein chains

367 a.a. *

Ligands

SO4 ×2

HEM-PIM ×2

Metals

_ZN

Waters ×619

* Residue conservation analysis

PDB id:

1f4t

Name:

Oxidoreductase

Title:

Thermophilic p450: cyp119 from sulfolobus solfactaricus with 4- phenylimidazole bound

Structure:

Cytochrome p450 119. Chain: a, b. Synonym: cyp119. Engineered: yes

Source:

Sulfolobus solfataricus. Organism_taxid: 2287. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.93Å R-factor: 0.225 R-free: 0.274

Authors:

J.K.Yano,L.S.Koo,D.J.Schuller,H.Li,P.R.Ortiz De Montellano,T.L.Poulos

Key ref:

J.K.Yano et al. (2000). Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus. J Biol Chem, 275, 31086-31092. PubMed id: 10859321 DOI: 10.1074/jbc.M004281200

Date:

09-Jun-00 Release date: 23-Oct-00

Protein chains

Q55080  (CP119_SULAC) -  Cytochrome P450 119 from Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)

Seq: 368 a.a.

Struc: 367 a.a.

Enzyme reactions

• Enzyme class 1: E.C.1.11.1.7 - peroxidase.
• Reaction: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
• Cofactor: Heme

Heme (Bound ligand (Het Group name = HEM) matches with 95.45% similarity)

• Enzyme class 2: E.C.1.14.-.-

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1074/jbc.M004281200

J Biol Chem 275:31086-31092 (2000)

PubMed id: 10859321

Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus.

J.K.Yano, L.S.Koo, D.J.Schuller, H.Li, P.R.Ortiz de Montellano, T.L.Poulos.

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.

Selected figure(s)

Figure 1.
Fig. 1. Ribbon diagram of CYP119 with 4-phenylimidazole ligated to the heme group. Helices are represented by white cylinders whereas -structures are represented by thick gray arrows. All figures were prepared with the program MOLSCRIPT (37) or SETOR (38) and rendered in Raster3D (39).

Figure 6.
Fig. 6. Ribbon diagram of the F-G region of CYP119. The F-G region encompasses residues 134-183. The white strand represents the F-G region of the imidazole-bound CYP119 structure. The gray strand represents the F-G region of the 4-phenylimidazole-bound structure. This representation shows the unwrapping of the F helix to accommodate the smaller imidazole ligand.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2000, 275, 31086-31092) copyright 2000.

Figures were selected by an automated process.