6FRW
X-ray structure of the levansucrase from Erwinia tasmaniensis
6FRW の概要
| エントリーDOI | 10.2210/pdb6frw/pdb |
| 分子名称 | Levansucrase (Beta-D-fructofuranosyl transferase), GLYCEROL, ZINC ION, ... (4 entities in total) |
| 機能のキーワード | fructosyltransferase, sucrose hydrolase, fructans production, transferase |
| 由来する生物種 | Erwinia tasmaniensis |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 46832.95 |
| 構造登録者 | Polsinelli, I.,Salomone-Stagni, M.,Caliandro, R.,Demitri, N.,Benini, S. (登録日: 2018-02-16, 公開日: 2019-02-06, 最終更新日: 2024-05-08) |
| 主引用文献 | Polsinelli, I.,Caliandro, R.,Salomone-Stagni, M.,Demitri, N.,Rejzek, M.,Field, R.A.,Benini, S. Comparison of the Levansucrase from the epiphyte Erwinia tasmaniensis vs its homologue from the phytopathogen Erwinia amylovora. Int. J. Biol. Macromol., 127:496-501, 2019 Cited by PubMed Abstract: Erwinia tasmaniensis is an epiphytic bacterium related to the plant pathogen Erwinia amylovora, the etiological agent of fire blight. In this study the levansucrase from E. tasmaniensis (EtLsc) has been compared with the homologous enzyme from E. amylovora (EaLsc). We characterized the enzymatic activity and compared the products profile of both enzymes by High Performance Anion Exchange Chromatography coupled with Pulsed Amperometric Detector (HPAEC-PAD). Moreover we determined the crystal structure of EtLsc to understand the structural peculiarity causing the different product profiles of the two homologues. EtLsc exhibits increased efficiency in the production of FOS, resulting in a better catalyst for biotechnological synthesis than EaLsc. Based on our results, we propose that the role of this enzyme in the life cycle of the two bacteria is most likely related to survival, rather than linked to pathogenicity in E. amylovora. PubMed: 30660564DOI: 10.1016/j.ijbiomac.2019.01.074 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.52 Å) |
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