5IQT

WelO5 bound to Fe(II), Cl, 2-oxoglutarate, and 12-epifischerindole U

Summary for 5IQT

• Entry DOI: 10.2210/pdb5iqt/pdb
• Related: 5IQS 5IQU 5IQV
• Descriptor: WelO5, FE (II) ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: metalloenzyme halogenase 2-oxoglutarate, oxidoreductase
• Biological source: Hapalosiphon welwitschii UTEX B 1830
• Total number of polymer chains: 3
• Total formula weight: 107914.91

Authors

Mitchell, A.J.,Boal, A.K. (deposition date: 2016-03-11, release date: 2016-06-29, Last modification date: 2023-09-27)

Primary citation

Mitchell, A.J.,Zhu, Q.,Maggiolo, A.O.,Ananth, N.R.,Hillwig, M.L.,Liu, X.,Boal, A.K.
Structural basis for halogenation by iron- and 2-oxo-glutarate-dependent enzyme WelO5.
Nat.Chem.Biol., 12:636-640, 2016

PubMed Abstract: 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 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.

PubMed: 27348090
DOI: 10.1038/nchembio.2112

Experimental method

X-RAY DIFFRACTION (2.4 Å)