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Updated: Jun 21, 2026

Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
The polyketide cyclase RemF from Streptomyces resistomycificus contains an unusual octahedral zinc binding site
Laura Silvennoinen1, Tatyana Sandalova, Gunter Schneider
1Department of Medical Biophysics and Biochemistry, Karolinska Institutet, Stockholm, Sweden.
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 A resolution. The enzyme subunit shows a beta-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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