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PDBsum entry 1f4t
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Oxidoreductase
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PDB id
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1f4t
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of a thermophilic cytochrome p450 from the archaeon sulfolobus solfataricus.
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Authors
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J.K.Yano,
L.S.Koo,
D.J.Schuller,
H.Li,
P.R.Ortiz de montellano,
T.L.Poulos.
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Ref.
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J Biol Chem, 2000,
275,
31086-31092.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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).
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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.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2000,
275,
31086-31092)
copyright 2000.
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