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PDBsum entry 3e5k
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Oxidoreductase
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PDB id
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3e5k
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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 structures of cytochrome p450 105p1 from streptomyces avermitilis: conformational flexibility and histidine ligation state.
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Authors
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L.H.Xu,
S.Fushinobu,
H.Ikeda,
T.Wakagi,
H.Shoun.
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Ref.
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J Bacteriol, 2009,
191,
1211-1219.
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PubMed id
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Abstract
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The polyene macrolide antibiotic filipin is widely used as a probe for
cholesterol in biological membranes. The filipin biosynthetic pathway of
Streptomyces avermitilis contains two position-specific hydroxylases,
C26-specific CYP105P1 and C1'-specific CYP105D6. In this study, we describe the
three X-ray crystal structures of CYP105P1: the ligand-free wild-type (WT-free),
4-phenylimidazole-bound wild-type (WT-4PI), and ligand-free H72A mutant
(H72A-free) forms. The BC loop region in the WT-free structure has a unique
feature; the side chain of His72 within this region is ligated to the heme iron.
On the other hand, this region is highly disordered and widely open in WT-4PI
and H72A-free structures, respectively. Histidine ligation of wild-type CYP105P1
was not detectable in solution, and a type II spectral change was clearly
observed when 4-phenylimidazole was titrated. The H72A mutant showed
spectroscopic characteristics that were almost identical to those of the
wild-type protein. In the H72A-free structure, there is a large pocket that is
of the same size as the filipin molecule. The highly flexible feature of the BC
loop region of CYP105P1 may be required to accept a large hydrophobic substrate.
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