Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The polyketide cyclase RemF from Streptomyces resistomycificus contains an unusual octahedral zinc binding site.,Silvennoinen L, Sandalova T, Schneider G FEBS Lett. 2009 Sep 3;583(17):2917-21. Epub 2009 Aug 6. PMID:19665022[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Silvennoinen L, Sandalova T, Schneider G. The polyketide cyclase RemF from Streptomyces resistomycificus contains an unusual octahedral zinc binding site. FEBS Lett. 2009 Sep 3;583(17):2917-21. Epub 2009 Aug 6. PMID:19665022 doi:10.1016/j.febslet.2009.07.061
