The polyketide cyclase RemF from Streptomyces resistomycificus contains an unusual octahedral zinc binding site |
| |
Authors: | Laura Silvennoinen |
| |
Affiliation: | Department of Medical Biophysics and Biochemistry, Karolinska Institutet, S-171 77 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 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. |
| |
Keywords: | Polyketide cyclase Zinc coordination Metalloprotein Protein crystallography Resistomycin |
本文献已被 ScienceDirect 等数据库收录! |