6A40
complex structure of Alginate lyase AlyF-OU02 with G4
6A40 の概要
| エントリーDOI | 10.2210/pdb6a40/pdb |
| 分子名称 | alginate lyase AlyF-OU02, alpha-L-gulopyranuronic acid-(1-4)-alpha-L-gulopyranuronic acid-(1-4)-alpha-L-gulopyranuronic acid-(1-4)-alpha-L-gulopyranuronic acid (3 entities in total) |
| 機能のキーワード | pl6, complex structure, cazy, lyase |
| 由来する生物種 | Vibrio splendidus |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 59803.30 |
| 構造登録者 | |
| 主引用文献 | Lyu, Q.,Zhang, K.,Shi, Y.,Li, W.,Diao, X.,Liu, W. Structural insights into a novel Ca2+-independent PL-6 alginate lyase from Vibrio OU02 identify the possible subsites responsible for product distribution. Biochim Biophys Acta Gen Subj, 1863:1167-1176, 2019 Cited by PubMed Abstract: Alginate lyases have a wide range of industrial applications, such as oligosaccharide preparation, medical treatment, and bioconversion. Therefore, the discovery and characterization of novel alginate lyases are extremely important. PL-6 alginate lyases are classified into two groups: those with a single domain or two domains. However, only one structure of a two-domain alginate lyase has been determined to date. In this study, we characterized a novel single-domain PL-6 alginate lyase (named AlyF). According to the biochemical analysis, AlyF possesses unique features compared with other PL-6 enzymes, including (1) a Ca-independent catalytic mechanism and (2) a PolyG-specific cleavage specificity that predominantly produces trisaccharides. The structures of AlyF and its complexes described here reveal the structural basis for these unique features and substrate binding mechanisms, which were further confirmed using mutagenesis. More importantly, we determined the possible subsites specifying the predominantly trisaccharide products of AlyF, which may facilitate the rational design of AlyF for potential applications in preparing a single alginate oligomer. PubMed: 31004719DOI: 10.1016/j.bbagen.2019.04.013 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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