4BG2
X-ray Crystal Structure of PatF from Prochloron didemni
Summary for 4BG2
| Entry DOI | 10.2210/pdb4bg2/pdb |
| Descriptor | PATF (2 entities in total) |
| Functional Keywords | transferase, patellamide, cyanobactins, natural products, prenyl transferases |
| Biological source | PROCHLORON DIDEMNI |
| Total number of polymer chains | 2 |
| Total formula weight | 74380.88 |
| Authors | Bent, A.F.,Koehnke, J.,Houssen, W.E.,Smith, M.C.M.,Jaspars, M.,Naismith, J.H. (deposition date: 2013-03-22, release date: 2013-04-03, Last modification date: 2024-10-09) |
| Primary citation | Bent, A.F.,Koehnke, J.,Houssen, W.E.,Smith, M.C.M.,Jaspars, M.,Naismith, J.H. Structure of Patf from Prochloron Didemni. Acta Crystallogr.,Sect.F, 69:618-, 2013 Cited by PubMed Abstract: Patellamides are macrocyclic peptides with potent biological effects and are a subset of the cyanobactins. Cyanobactins are natural products that are produced by a series of enzymatic transformations and a common modification is the addition of a prenyl group. Puzzlingly, the pathway for patellamides in Prochloron didemni contains a gene, patF, with homology to prenylases, but patellamides are not themselves prenylated. The structure of the protein PatF was cloned, expressed, purified and determined. Prenylase activity could not be demonstrated for the protein, and examination of the structure revealed changes in side-chain identity at the active site. It is suggested that these changes have inactivated the protein. Attempts to mutate these residues led to unfolded protein. PubMed: 23722837DOI: 10.1107/S1744309113012931 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.13 Å) |
Structure validation
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