Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis

Leah C. Blasiak, Frédéric H. Vaillancourt, Christopher T. Walsh and Catherine L. Drennan ()
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Leah C. Blasiak: Massachusetts Institute of Technology
Frédéric H. Vaillancourt: Harvard Medical School
Christopher T. Walsh: Harvard Medical School
Catherine L. Drennan: Massachusetts Institute of Technology

Nature, 2006, vol. 440, issue 7082, 368-371

Abstract: Abstract Non-haem Fe(ii)/α-ketoglutarate (αKG)-dependent enzymes harness the reducing power of αKG to catalyse oxidative reactions, usually the hydroxylation of unactivated carbons, and are involved in processes such as natural product biosynthesis, the mammalian hypoxic response, and DNA repair1,2. These enzymes couple the decarboxylation of αKG with the formation of a high-energy ferryl-oxo intermediate that acts as a hydrogen-abstracting species2,3,4. All previously structurally characterized mononuclear iron enzymes contain a 2-His, 1-carboxylate motif that coordinates the iron1,2. The two histidines and one carboxylate, known as the ‘facial triad’, form one triangular side of an octahedral iron coordination geometry. A subclass of mononuclear iron enzymes has been shown to catalyse halogenation reactions, rather than the more typical hydroxylation reaction5,6. SyrB2, a member of this subclass, is a non-haem Fe(ii)/αKG-dependent halogenase that catalyses the chlorination of threonine in syringomycin E biosynthesis5. Here we report the structure of SyrB2 with both a chloride ion and αKG coordinated to the iron ion at 1.6 Å resolution. This structure reveals a previously unknown coordination of iron, in which the carboxylate ligand of the facial triad is replaced by a chloride ion.

Date: 2006
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DOI: 10.1038/nature04544

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