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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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Contents |
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* Residue conservation analysis
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J Bacteriol
191:1211-1219
(2009)
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PubMed id:
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Crystal structures of cytochrome P450 105P1 from Streptomyces avermitilis: conformational flexibility and histidine ligation state.
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L.H.Xu,
S.Fushinobu,
H.Ikeda,
T.Wakagi,
H.Shoun.
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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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S.Takamatsu,
L.H.Xu,
S.Fushinobu,
H.Shoun,
M.Komatsu,
D.E.Cane,
and
H.Ikeda
(2011).
Pentalenic acid is a shunt metabolite in the biosynthesis of the pentalenolactone family of metabolites: hydroxylation of 1-deoxypentalenic acid mediated by CYP105D7 (SAV_7469) of Streptomyces avermitilis.
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J Antibiot (Tokyo),
64,
65-71.
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Y.T.Lee,
E.C.Glazer,
R.F.Wilson,
C.D.Stout,
and
D.B.Goodin
(2011).
Three clusters of conformational states in p450cam reveal a multistep pathway for closing of the substrate access channel.
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Biochemistry,
50,
693-703.
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Z.Li,
S.G.Rupasinghe,
M.A.Schuler,
and
S.K.Nair
(2011).
Crystal structure of a phenol-coupling P450 monooxygenase involved in teicoplanin biosynthesis.
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Proteins,
79,
1728-1738.
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PDB code:
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T.C.Pochapsky,
S.Kazanis,
and
M.Dang
(2010).
Conformational plasticity and structure/function relationships in cytochromes P450.
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Antioxid Redox Signal,
13,
1273-1296.
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Y.T.Lee,
R.F.Wilson,
I.Rupniewski,
and
D.B.Goodin
(2010).
P450cam visits an open conformation in the absence of substrate.
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Biochemistry,
49,
3412-3419.
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PDB codes:
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K.T.Gagnon,
S.Y.Ju,
M.B.Goshe,
E.S.Maxwell,
and
S.Franzen
(2009).
A role for hydrophobicity in a Diels-Alder reaction catalyzed by pyridyl-modified RNA.
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Nucleic Acids Res,
37,
3074-3082.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
