Structural basis for halogenation by iron- and 2-oxo-glutarate-dependent enzyme WelO5.
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SUBMITTER: Mitchell AJ
PROVIDER: S-EPMC5391150 | biostudies-literature | 2016 Aug
REPOSITORIES: biostudies-literature
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Structural basis for halogenation by iron- and 2-oxo-glutarate-dependent enzyme WelO5.
Mitchell Andrew J AJ Zhu Qin Q Maggiolo Ailiena O AO Ananth Nikhil R NR Hillwig Matthew L ML Liu Xinyu X Boal Amie K AK
Nature chemical biology 20160627 8
A 2.4-Å-resolution X-ray crystal structure of the carrier-protein-independent halogenase WelO5 in complex with its welwitindolinone precursor substrate, 12-epi-fischerindole U, reveals that the C13 chlorination target is proximal to the anticipated site of the oxo group in a presumptive cis-halo-oxo-iron(IV) (haloferryl) intermediate. Prior study of related halogenases forecasts substrate hydroxylation in this active-site configuration, but X-ray crystallographic verification of C13 halogenation ...[more]
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