4BG2
X-ray Crystal Structure of PatF from Prochloron didemni
4BG2 の概要
| エントリーDOI | 10.2210/pdb4bg2/pdb |
| 分子名称 | PATF (2 entities in total) |
| 機能のキーワード | transferase, patellamide, cyanobactins, natural products, prenyl transferases |
| 由来する生物種 | PROCHLORON DIDEMNI |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 74380.88 |
| 構造登録者 | Bent, A.F.,Koehnke, J.,Houssen, W.E.,Smith, M.C.M.,Jaspars, M.,Naismith, J.H. (登録日: 2013-03-22, 公開日: 2013-04-03, 最終更新日: 2024-10-09) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.13 Å) |
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