3HT2
Zink containing polyketide cyclase RemF from Streptomyces resistomycificus
Summary for 3HT2
| Entry DOI | 10.2210/pdb3ht2/pdb |
| Related | 3HT1 |
| Descriptor | RemF protein, ZINC ION (3 entities in total) |
| Functional Keywords | cupin fold, zn-binding, antibiotic biosynthesis, resistomycin, metalloprotein, cyclase, lyase |
| Biological source | Streptomyces resistomycificus |
| Total number of polymer chains | 2 |
| Total formula weight | 33272.84 |
| Authors | Silvennoinen, L.,Sandalova, T.,Schneider, G. (deposition date: 2009-06-11, release date: 2009-10-13, Last modification date: 2024-11-20) |
| Primary citation | Silvennoinen, L.,Sandalova, T.,Schneider, G. The polyketide cyclase RemF from Streptomyces resistomycificus contains an unusual octahedral zinc binding site Febs Lett., 583:2917-2921, 2009 Cited by PubMed 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. PubMed: 19665022DOI: 10.1016/j.febslet.2009.07.061 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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