8X2V
Crystal structure of the ancestral GH19 chitinase, Anc4+LoopII (P12K/N13H mutant)
8X2V の概要
| エントリーDOI | 10.2210/pdb8x2v/pdb |
| 分子名称 | GH19 chitinase (2 entities in total) |
| 機能のキーワード | gh19 chitinase, hydrolase |
| 由来する生物種 | synthetic construct |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 25461.28 |
| 構造登録者 | |
| 主引用文献 | Kozome, D.,Sljoka, A.,Laurino, P. Remote loop evolution reveals a complex biological function for chitinase enzymes beyond the active site. Nat Commun, 15:3227-3227, 2024 Cited by PubMed Abstract: Loops are small secondary structural elements that play a crucial role in the emergence of new enzyme functions. However, the evolutionary molecular mechanisms how proteins acquire these loop elements and obtain new function is poorly understood. To address this question, we study glycoside hydrolase family 19 (GH19) chitinase-an essential enzyme family for pathogen degradation in plants. By revealing the evolutionary history and loops appearance of GH19 chitinase, we discover that one loop which is remote from the catalytic site, is necessary to acquire the new antifungal activity. We demonstrate that this remote loop directly accesses the fungal cell wall, and surprisingly, it needs to adopt a defined structure supported by long-range intramolecular interactions to perform its function. Our findings prove that nature applies this strategy at the molecular level to achieve a complex biological function while maintaining the original activity in the catalytic pocket, suggesting an alternative way to design new enzyme function. PubMed: 38622119DOI: 10.1038/s41467-024-47588-8 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.29 Å) |
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