Abstract

The objective of this research is to determine the molecular structure of ubiquitin, using protein x-ray crystallographic techniques. This small protein has been sequenced and has a molecular weight of 8565 daltons. Although its exact role in the cell is unknown, it has been implicated in transcription and intracellular ATP-dependent protein degradation. These two functions involve the formation of ubiquitin-protein conjugates. The polypeptide chain has been traced, and the structure has been determined at 2.8 Angstrom resolution. Refinement of the structure at the highest possible resolution (approximately 1.0 Angstrom) is the ultimate goal. Crystals of yeast ubiquitin have been grown, and comparison of the structures of mammalian ubiquitin and yeast ubiquitin will also be undertaken as the refinement progresses.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM027144-08
Application #
3274558
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1979-12-01
Project End
1989-03-31
Budget Start
1987-04-01
Budget End
1988-03-31
Support Year
8
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
University of Alabama Birmingham
Department
Type
School of Medicine & Dentistry
DUNS #
004514360
City
Birmingham
State
AL
Country
United States
Zip Code
35294

  Publications

Vijay-Kumar, S; Bugg, C E; Cook, W J (1987) Structure of ubiquitin refined at 1.8 A resolution. J Mol Biol 194:531-44
Vijay-Kumar, S; Bugg, C E; Wilkinson, K D et al. (1987) Comparison of the three-dimensional structures of human, yeast, and oat ubiquitin. J Biol Chem 262:6396-9
Vijay-Kumar, S; Bugg, C E; Wilkinson, K D et al. (1985) Three-dimensional structure of ubiquitin at 2.8 A resolution. Proc Natl Acad Sci U S A 82:3582-5