Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2048406 | FEBS Letters | 2009 | 5 Pages |
Abstract
RemF is a polyketide cyclase involved in the biosynthesis of the aromatic pentacyclic metabolite resistomycin in Streptomyces resistomycificus. The enzyme is a member of a structurally hitherto uncharacterized class of polyketide cyclases. The crystal structure of RemF was determined by SAD and refined to 1.2 Å resolution. The enzyme subunit shows a β-sandwich structure with a topology characteristic for the cupin fold. RemF contains a metal binding site located at the bottom of the predominantly hydrophobic active site cavity. A zinc ion is coordinated to four histidine side chains, and two water molecules in octahedral ligand sphere geometry, highly unusual for zinc binding sites in proteins.
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Authors
Laura Silvennoinen, Tatyana Sandalova, Gunter Schneider,