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PDBsum entry 3pvr
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Oxidoreductase
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PDB id
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3pvr
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Contents |
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304 a.a.
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236 a.a.
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248 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural and functional studies of the escherichia coli phenylacetyl-Coa monooxygenase complex.
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Authors
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A.M.Grishin,
E.Ajamian,
L.Tao,
L.Zhang,
R.Menard,
M.Cygler.
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Ref.
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J Biol Chem, 2011,
286,
10735-10743.
[DOI no: ]
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PubMed id
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Abstract
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The utilization of phenylacetic acid (PA) in Escherichia coli occurs through a
hybrid pathway that shows features of both aerobic and anaerobic metabolism.
Oxygenation of the aromatic ring is performed by a multisubunit
phenylacetyl-coenzyme A oxygenase complex that shares remote homology of two
subunits to well studied bacterial multicomponent monooxygenases and was
postulated to form a new bacterial multicomponent monooxygenase subfamily. We
expressed the subunits PaaA, B, C, D, and E of the PA-CoA oxygenase and showed
that PaaABC, PaaAC, and PaaBC form stable subcomplexes that can be purified. In
vitro reconstitution of the oxygenase subunits showed that each of the PaaA, B,
C, and E subunits are necessary for catalysis, whereas PaaD is not essential. We
have determined the crystal structure of the PaaAC complex in a ligand-free form
and with several CoA derivatives. We conclude that PaaAC forms a catalytic core
with a monooxygenase fold with PaaA being the catalytic α subunit and PaaC, the
structural β subunit. PaaAC forms heterotetramers that are organized very
differently from other known multisubunit monooxygenases and lacks their
conservative network of hydrogen bonds between the di-iron center and protein
surface, suggesting different association with the reductase and different
mechanisms of electron transport. The PaaA structure shows adaptation of the
common access route to the active site for binding a CoA-bound substrate. The
enzyme-substrate complex shows the orientation of the aromatic ring, which is
poised for oxygenation at the ortho-position, in accordance with the expected
chemistry. The PA-CoA oxygenase complex serves as a paradigm for the new
subfamily multicomponent monooxygenases comprising several hundred homologs.
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