Structural highlights
Function
A0A067YX61_9CYAN
Publication Abstract from PubMed
A 2.4-A-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 in single crystals mandates that ligand dynamics must reposition the oxygen ligand to enable the observed outcome. S189A WelO5 produces a mixture of halogenation and hydroxylation products, showing that an outer-sphere hydrogen-bonding group orchestrates ligand movements to achieve a configuration that promotes halogen transfer.
Structural basis for halogenation by iron- and 2-oxo-glutarate-dependent enzyme WelO5.,Mitchell AJ, Zhu Q, Maggiolo AO, Ananth NR, Hillwig ML, Liu X, Boal AK Nat Chem Biol. 2016 Jun 27. doi: 10.1038/nchembio.2112. PMID:27348090[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mitchell AJ, Zhu Q, Maggiolo AO, Ananth NR, Hillwig ML, Liu X, Boal AK. Structural basis for halogenation by iron- and 2-oxo-glutarate-dependent enzyme WelO5. Nat Chem Biol. 2016 Jun 27. doi: 10.1038/nchembio.2112. PMID:27348090 doi:http://dx.doi.org/10.1038/nchembio.2112
