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Science 1 September 2000:
Vol. 289. no. 5484, pp. 1546 - 1550
DOI: 10.1126/science.289.5484.1546
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Reports

Structural Evidence for Evolution of the beta /alpha Barrel Scaffold by Gene Duplication and Fusion

Dietmar Lang,1 Ralf Thoma,2 Martina Henn-Sax,3 Reinhard Sterner,234 Matthias Wilmanns1*

The atomic structures of two proteins in the histidine biosynthesis pathway consist of beta /alpha 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.

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.
*   To whom correspondence should be addressed. E-mail: wilmanns{at}embl-hamburg.de

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