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Molecular handcraft of a well‐folded protein chimera

Title data

Toledo‐Patiño, Saacnicteh ; Goetz, Sara Kathrin ; Shanmugaratnam, Sooruban ; Höcker, Birte ; Farías‐Rico, José Arcadio:
Molecular handcraft of a well‐folded protein chimera.
In: FEBS Letters. (20 March 2024) .
ISSN 1873-3468
DOI: https://doi.org/10.1002/1873-3468.14856

Abstract in another language

Modular assembly is a compelling pathway to create new proteins, a concept supported by protein engineering and millennia of evolution. Natural evolution provided a repository of building blocks, known as domains, which trace back to even shorter segments that underwent numerous 'copy-paste' processes culminating in the scaffolds we see today. Utilizing the subdomain-database Fuzzle, we constructed a fold-chimera by integrating a flavodoxin-like fragment into a periplasmic binding protein. This chimera is well-folded and a crystal structure reveals stable interfaces between the fragments. These findings demonstrate the adaptability of α/β-proteins and offer a stepping stone for optimization. By emphasizing the practicality of fragment databases, our work pioneers new pathways in protein engineering. Ultimately, the results substantiate the conjecture that periplasmic binding proteins originated from a flavodoxin-like ancestor.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: chimeric proteins; homology; protein engineering; protein fold evolution; sequence‐based analysis; sub‐domain
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry III - Protein Design > Chair Biochemistry III - Protein Design - Univ.-Prof. Dr. Birte Höcker
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry III - Protein Design
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 500 Natural sciences
500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 16 May 2024 05:40
Last Modified: 16 May 2024 05:40
URI: https://eref.uni-bayreuth.de/id/eprint/89560