Structural Evidence for Evolution of the β/α Barrel Scaffold by Gene Duplication and Fusion

Author:

Lang Dietmar1,Thoma Ralf2,Henn-Sax Martina3,Sterner Reinhard234,Wilmanns Matthias1

Affiliation:

1. European Molecular Biology Laboratory (EMBL) Hamburg Outstation, EMBL c/o Deutsches Elektronen- Synchrotron (DESY), Notkestrasse 85, D-22603 Hamburg, Germany.

2. Abteilung für Biophysikalische Chemie, Biozentrum der Universität Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.

3. Abteilung für molekulare Genetik und Präparative Molekularbiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Grisebachstrasse 8, D-37077 Göttingen, Germany.

4. Universität zu Köln, Institut für Biochemie, Otto-Fischer-Strasse 12-14, D-50674 Köln, Germany.

Abstract

The atomic structures of two proteins in the histidine biosynthesis pathway consist of β/α barrels with a twofold repeat pattern. It is likely that these proteins evolved by twofold gene duplication and gene fusion from a common half-barrel ancestor. These ancestral domains are not visible as independent domains in the extant proteins but can be inferred from a combination of sequence and structural analysis. The detection of subdomain structures may be useful in efforts to search genome sequences for functionally and structurally related proteins.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference47 articles.

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