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Secondary Structure of Uracil-DNA Glycosylase Inhibitor Protein

Authors :
Richard D. Beger
Suganthi Balasubramanian
Philip H. Bolton
Dale W. Mosbaugh
Samuel E. Bennett
Source :
Journal of Biological Chemistry. 270:296-303
Publication Year :
1995
Publisher :
Elsevier BV, 1995.

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.

Details

ISSN :
00219258 and 11631171
Volume :
270
Database :
OpenAIRE
Journal :
Journal of Biological Chemistry
Accession number :
edsair.doi.dedup.....da183132e7cf277e503e8d7f97596808
Full Text :
https://doi.org/10.1074/jbc.270.1.296