8hnj

Domain-stabilized glutamine-binding protein

spinqualitylabelsall models 8hnj, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8hnj is a 6 chain structure with sequence from Escherichia coli 908519. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.03Å Ligands: GLN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLNH_ECOLI Involved in a glutamine-transport system GlnHPQ. Publication Abstract from PubMed 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. Domain-wise dissection of thermal stability enhancement in multidomain proteins.,Oh J, Durai P, Kannan P, Park J, Yeon YJ, Lee WK, Park K, Seo MH Int J Biol Macromol. 2023 May 15;237:124141. doi: 10.1016/j.ijbiomac.2023.124141. , Epub 2023 Mar 21. PMID:36958447 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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