Kuper, Jochen and Doenges, Catharina and Wilmanns, Matthias (2005) Two-fold repeated (beta alpha)(4) half-barrels may provide a molecular tool for dual substrate specificity. EMBO REPORTS, 6 (2). pp. 134-139. ISSN 1469-221X, 1469-3178
Full text not available from this repository. (Request a copy)Abstract
Some bacterial genomes contain an incomplete set of genes encoding phosphoribosyl isomerases, raising the question of whether there exists broadened substrate specificity for the missing gene products. To investigate the underlying molecular principles of this hypothesis, we have determined the crystal structure of the bifunctional enzyme PriA from Streptomyces coelicolor at 1.8 Angstrom resolution. It consists of a (betaalpha)(8)-barrel fold that is assembled by two symmetric (betaalpha)(4) half-barrels. The structure shows how its active site may catalyse the isomerization reactions of two different substrates, and we provide a plausible model of how the smaller of the two substrates could be bound in two different orientations. Our findings expand the half-barrel ancestor concept by demonstrating that symmetry-related half-barrels could provide a smart solution to cope with dual substrate specificity. The data may help to unravel molecular rationales regarding how organisms with miniature genomes can keep central biological pathways functional.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PHOSPHORIBOSYL ANTHRANILATE ISOMERASE; TRYPTOPHAN BIOSYNTHESIS; SEQUENCE ALIGNMENTS; METABOLIC PATHWAYS; ENZYMES; EVOLUTION; HISTIDINE; PROTEIN; CONSERVATION; SYNTHASE; phosphoribosyl isomerase; evolution of (beta alpha)(8) barrels; tryptophan and histidine biosynthesis |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 31 May 2021 05:23 |
| Last Modified: | 31 May 2021 05:23 |
| URI: | https://pred.uni-regensburg.de/id/eprint/36513 |
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