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PMID: 7814390 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Secondary structure of uracil-DNA glycosylase inhibitor protein.

The Journal of biological chemistry ·Vol. 270 ·No. 1 ·1995-01-06 ·Pages 296-303

Balasubramanian S, Beger RD, Bennett SE, Mosbaugh DW, Bolton PH

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.

MeSH Terms
Amino Acid Sequence Hydrogen-Ion Concentration Magnetic Resonance Spectroscopy Molecular Sequence Data Protein Structure, Secondary Viral Proteins/chemistry
Chemicals
Viral Proteins uracil-DNA glycosylase inhibitor protein, B. subtilis bacteriophage
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Balasubramanian S
Chemistry Department, Wesleyan University, Middletown, Connecticut 06450.
Beger R D
Bennett S E
Mosbaugh D W
Bolton P H
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1995-01-06
Pages
296-303
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIEHS NIH HHS · ES 00210 · United States
NIGMS NIH HHS · GM 32823 · United States
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