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Diversifying de novo TIM barrels by hallucination

Title data

Beck, Julian ; Shanmugaratnam, Sooruban ; Höcker, Birte:
Diversifying de novo TIM barrels by hallucination.
In: Protein Science. Vol. 33 (June 2024) Issue 6 . - e5001.
ISSN 1469-896X

Abstract in another language

De novo protein design expands the protein universe by creating new sequences to accomplish tailor-made enzymes in the future. A promising topology to implement diverse enzyme functions is the ubiquitous TIM-barrel fold. Since the initial de novo design of an idealized four-fold symmetric TIM barrel, the family of de novo TIM barrels is expanding rapidly. Despite this and in contrast to natural TIM barrels, these novel proteins lack cavities and structural elements essential for the incorporation of binding sites or enzymatic functions. In this work, we diversified a de novo TIM barrel by extending multiple βα-loops using constrained hallucination. Experimentally tested designs were found to be soluble upon expression in Escherichia coli and well-behaved. Biochemical characterization and crystal structures revealed successful extensions with defined α-helical structures. These diversified de novo TIM barrels provide a framework to explore a broad spectrum of functions based on the potential of natural TIM barrels.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: (βα)8‐barrel; de novo protein design; hallucination; machine learning; small molecule binding site
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
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 07:21
Last Modified: 16 May 2024 07:21