SECONDARY STRUCTURE OF URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN

被引:12
作者
BALASUBRAMANIAN, S
BEGER, RD
BENNETT, SE
MOSBAUGH, DW
BOLTON, PH
机构
[1] WESLEYAN UNIV,DEPT CHEM,MIDDLETOWN,CT 06450
[2] OREGON STATE UNIV,DEPT AGR CHEM,CORVALLIS,OR 97331
[3] OREGON STATE UNIV,DEPT BIOCHEM & BIOPHYS,CORVALLIS,OR 97331
[4] OREGON STATE UNIV,CTR ENVIRONM HLTH SCI,CORVALLIS,OR 97331
关键词
D O I
10.1074/jbc.270.1.296
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:296 / 303
页数:8
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