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. 1995 Jan 6;270(1):296-303.
doi: 10.1074/jbc.270.1.296.

Secondary structure of uracil-DNA glycosylase inhibitor protein

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Free article

Secondary structure of uracil-DNA glycosylase inhibitor protein

S Balasubramanian et al. J Biol Chem. .
Free article

Abstract

The Bacillus subtilis bacteriophage PBS2 uracil-DNA glycosylase inhibitor (Ugi) is an acidic protein of 84 amino acids that inactivates uracil-DNA glycosylase from diverse organisms (Wang, Z., and Mosbaugh, D. W. (1989) J. Biol. Chem. 264, 1163-1171). The secondary structure of Ugi has been determined by solution state multidimensional nuclear magnetic resonance. The protein adopts a single well defined structure consisting of five anti-parallel beta-strands and two alpha-helices. Six loop or turn regions were identified that contain approximately one half of the acidic amino acid residues and connect the beta-strands sequentially to one another. The secondary structure suggests which regions of Ugi may be involved in interactions with uracil-DNA glycosylase.

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