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PDBsum entry 3awm
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Oxidoreductase
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PDB id
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3awm
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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 h2o2-Dependent cytochrome p450spalpha with its bound fatty acid substrate: insight into the regioselective hydroxylation of fatty acids at the alpha position.
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Authors
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T.Fujishiro,
O.Shoji,
S.Nagano,
H.Sugimoto,
Y.Shiro,
Y.Watanabe.
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Ref.
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J Biol Chem, 2011,
286,
29941-29950.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
90%.
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Abstract
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Cytochrome P450(SPα) (CYP152B1) isolated from Sphingomonas paucimobilis is the
first P450 to be classified as a H(2)O(2)-dependent P450. P450(SPα)
hydroxylates fatty acids with high α-regioselectivity. Herein we report the
crystal structure of P450(SPα) with palmitic acid as a substrate at a
resolution of 1.65 Å. The structure revealed that the C(α) of the bound
palmitic acid in one of the alternative conformations is 4.5 Å from the heme
iron. This conformation explains the highly selective α-hydroxylation of fatty
acid observed in P450(SPα). Mutations at the active site and the F-G loop of
P450(SPα) did not impair its regioselectivity. The crystal structures of
mutants (L78F and F288G) revealed that the location of the bound palmitic acid
was essentially the same as that in the WT, although amino acids at the active
site were replaced with the corresponding amino acids of cytochrome P450(BSβ)
(CYP152A1), which shows β-regioselectivity. This implies that the high
regioselectivity of P450(SPα) is caused by the orientation of the hydrophobic
channel, which is more perpendicular to the heme plane than that of P450(BSβ).
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