We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis.
- Authors
Blasiak, Leah C.; Vaillancourt, Frédéric H.; Walsh, Christopher T.; Drennan, Catherine L.
- 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 repair. These enzymes couple the decarboxylation of αKG with the formation of a high-energy ferryl-oxo intermediate that acts as a hydrogen-abstracting species. All previously structurally characterized mononuclear iron enzymes contain a 2-His, 1-carboxylate motif that coordinates the iron. 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 reaction. SyrB2, a member of this subclass, is a non-haem Fe(ii)/αKG-dependent halogenase that catalyses the chlorination of threonine in syringomycin E biosynthesis. 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.
- Subjects
ENZYMES; BIOSYNTHESIS; HYDROXYLATION; DNA; GEOMETRY; HALOGENATION
- Publication
Nature, 2006, Vol 440, Issue 7082, p368
- ISSN
0028-0836
- Publication type
Article
- DOI
10.1038/nature04544