Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Höcker B,Schmidt S,Sterner Rdoi
10.1016/s0014-5793(01)03232-xkeywords:
subject
Has Abstractpub_date
2002-01-16 00:00:00pages
133-5issue
3eissn
0014-5793issn
1873-3468pii
S001457930103232Xjournal_volume
510pub_type
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