8HNJ
Domain-stabilized glutamine-binding protein
8HNJ の概要
エントリーDOI | 10.2210/pdb8hnj/pdb |
分子名称 | Glutamine ABC transporter, periplasmic glutamine-binding protein GlnH, GLUTAMINE (3 entities in total) |
機能のキーワード | computationally stabilized, glutamine-binding protein, amino acid transport, domain engineered protein, transport protein |
由来する生物種 | Escherichia coli 908519 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 154128.34 |
構造登録者 | Choi, S.H.,Park, J.H.,Seo, M.H.,Park, K.W.,Lee, W.K. (登録日: 2022-12-08, 公開日: 2023-07-19, 最終更新日: 2024-05-29) |
主引用文献 | Oh, J.,Durai, P.,Kannan, P.,Park, J.,Yeon, Y.J.,Lee, W.K.,Park, K.,Seo, M.H. Domain-wise dissection of thermal stability enhancement in multidomain proteins. Int.J.Biol.Macromol., 237:124141-124141, 2023 Cited by PubMed Abstract: Stability is critical for the proper functioning of all proteins. Optimization of protein thermostability is a key step in the development of industrial enzymes and biologics. Herein, we demonstrate that multidomain proteins can be stabilized significantly using domain-based engineering followed by the recombination of the optimized domains. Domain-level analysis of designed protein variants with similar structures but different thermal profiles showed that the independent enhancement of the thermostability of a constituent domain improves the overall stability of the whole multidomain protein. The crystal structure and AlphaFold-predicted model of the designed proteins via domain-recombination provided a molecular explanation for domain-based stepwise stabilization. Our study suggests that domain-based modular engineering can minimize the sequence space for calculations in computational design and experimental errors, thereby offering useful guidance for multidomain protein engineering. PubMed: 36958447DOI: 10.1016/j.ijbiomac.2023.124141 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.03 Å) |
構造検証レポート
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