Crystallization and preliminary X-ray analysis of PaaAC, the main component of the hydroxylase of the Escherichia coli phenylacetyl-coenzyme A oxygenase complex

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DOIResolve DOI: http://doi.org/10.1107/S174430911002748X
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TypeArticle
Journal titleActa crystallographica section F
VolumeF66
Pages10451049; # of pages: 5
AbstractThe Escherichia coli paa operon encodes enzymes of the phenylacetic acidutilization pathway that metabolizes phenylacetate in the form of a coenzyme A (CoA) derivative. The phenylacetyl-coenzyme A oxygenase complex, which has been postulated to contain five components designated PaaABCDE, catalyzes ring hydroxylation of phenylacetyl-CoA. The PaaAC subcomplex shows low sequence similarity to other bacterial multicomponent monooxygenases (BMMs) and forms a separate branch on the phylogenetic tree. PaaAC, which catalyzes the hydroxylation reaction, was purified and crystallized in the absence of a bound ligand as well as in complexes with CoA, 3-hydroxybutyryl-CoA, benzoyl-CoA and the true substrate phenylacetyl-CoA. Crystals of the ligandfree enzyme belonged to space group P212121 and diffracted to 2.65 A resolution, whereas complexes with CoA and its derivatives crystallized in space group P41212 and diffracted to ~2.0 A resolution. PaaAC represents the first crystallized BMM hydroxylase that utilizes a CoA-linked substrate.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); NRC Biotechnology Research Institute
Peer reviewedYes
NRC number53126
NPARC number16512460
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Record identifier73325106-49b1-4037-9268-77a11d59d76a
Record created2010-12-14
Record modified2016-05-09
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