A common evolutionary origin of two elementary enzyme folds.

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 Lett

journal_title

FEBS letters

authors

Höcker B,Schmidt S,Sterner R

doi

10.1016/s0014-5793(01)03232-x

keywords:

subject

Has Abstract

pub_date

2002-01-16 00:00:00

pages

133-5

issue

3

eissn

0014-5793

issn

1873-3468

pii

S001457930103232X

journal_volume

510

pub_type

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