8HNJ

Domain-stabilized glutamine-binding protein

Summary for 8HNJ

• Entry DOI: 10.2210/pdb8hnj/pdb
• Descriptor: Glutamine ABC transporter, periplasmic glutamine-binding protein GlnH, GLUTAMINE (3 entities in total)
• Functional Keywords: computationally stabilized, glutamine-binding protein, amino acid transport, domain engineered protein, transport protein
• Biological source: Escherichia coli 908519
• Total number of polymer chains: 6
• Total formula weight: 154128.34

Authors

Choi, S.H.,Park, J.H.,Seo, M.H.,Park, K.W.,Lee, W.K. (deposition date: 2022-12-08, release date: 2023-07-19, Last modification date: 2024-05-29)

Primary citation

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

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: 36958447
DOI: 10.1016/j.ijbiomac.2023.124141

Experimental method

X-RAY DIFFRACTION (2.03 Å)