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Secondary Structure of Uracil-DNA Glycosylase Inhibitor Protein
- 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.
- Subjects :
- chemistry.chemical_classification
Magnetic Resonance Spectroscopy
biology
Chemistry
Molecular Sequence Data
Cell Biology
Bacillus subtilis
Inhibitor protein
Hydrogen-Ion Concentration
biology.organism_classification
Biochemistry
Protein Structure, Secondary
Protein tertiary structure
Amino acid
Turn (biochemistry)
Viral Proteins
DNA glycosylase
Uracil-DNA glycosylase
Amino Acid Sequence
Molecular Biology
Protein secondary structure
Subjects
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