at Google ScholarTitle data
Höcker, Birte ; Schmidt, Steffen ; Sterner, Reinhard:
A common evolutionary origin of two elementary enzyme folds.
In: FEBS Letters.
Vol. 510
(2002)
Issue 3
.
- pp. 133-135.
ISSN 1873-3468
DOI: https://doi.org/10.1016/S0014-5793(01)03232-X
Abstract in another language
The (beta alpha)(8)-barrel is the most frequent and most versatile fold among enzymes [Höcker et al., Curr. Opin. Biotechnol. 12 (2001) 376-381; Wierenga, FEBS Lett. 492 (2001) 193-198]. Structural and functional evidence suggests that (beta alpha)(8)-barrels evolved from an ancestral half-barrel, which consisted of four (beta alpha) units stabilized by dimerization [Lang et al., Science 289 (2000) 1546-550; Höcker et al., Nat. Struct. Biol. 8 (2001) 32-36; Gerlt and Babbitt, Nat. Struct. Biol. 8 (2001) 5-7]. Here, by performing a comprehensive database search, we detect a striking and unexpected structural and amino acid sequence similarity between (beta alpha)(4) half-barrels and members of the (beta alpha)(5) flavodoxin-like fold. These findings provoke the hypothesis that a large fraction of the modern-day enzymes evolved from a basic structural building block, which can be identified by a combination of sequence and structural analyses.
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 09:10 |
| Last Modified: | 05 Jun 2023 12:18 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/37216 |