Title data
Farías-Rico, José Arcadio ; Schmidt, Steffen ; Höcker, Birte:
Evolutionary relationship of two ancient protein superfolds.
In: Nature Chemical Biology.
Vol. 10
(2014)
Issue 9
.
- pp. 710-715.
ISSN 1552-4469
DOI: https://doi.org/10.1038/nchembio.1579
Abstract in another language
Proteins are the molecular machines of the cell that fold into specific three-dimensional structures to fulfill their functions. To improve our understanding of how the structure and function of proteins arises, it is crucial to understand how evolution has generated the structural diversity we observe today. Classically, proteins that adopt different folds are considered to be nonhomologous. However, using state-of-the-art tools for homology detection, we found evidence of homology between proteins of two ancient and highly populated protein folds, the (βα)8-barrel and the flavodoxin-like fold. We detected a family of sequences that show intermediate features between both folds and determined what is to our knowledge the first representative crystal structure of one of its members, giving new insights into the evolutionary link of two of the earliest folds. Our findings contribute to an emergent vision where protein superfolds share common ancestry and encourage further approaches to complete the mapping of structure space onto sequence space.
Further data
Item Type: | Article in a journal |
---|---|
Refereed: | Yes |
Institutions of the University: | Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Birte Höcker Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry |
Result of work at the UBT: | No |
DDC Subjects: | 500 Science 500 Science > 540 Chemistry |
Date Deposited: | 23 May 2017 09:06 |
Last Modified: | 27 Oct 2022 10:37 |
URI: | https://eref.uni-bayreuth.de/id/eprint/37215 |