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The polyketide cyclase RemF from Streptomyces resistomycificus contains an unusual octahedral zinc binding site
Author(s) -
Silvennoinen Laura,
Sandalova Tatyana,
Schneider Gunter
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.07.061
Subject(s) - polyketide , stereochemistry , chemistry , binding site , active site , cyclase , streptomyces , zinc , histidine , ligand (biochemistry) , enzyme , biochemistry , biosynthesis , biology , receptor , bacteria , organic chemistry , genetics
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.