Structure-function analysis of human protein Ero1-L{alpha}
- Department of Pharmaceutical Sciences, School of Pharmacy, East China University of Science and Technology, 130 Meilong Road, Shanghai 200237 (China)
Human Ero1-L{alpha} catalyzes the formation of disulfide bond and hence plays an essential role in protein folding. Understanding the mechanism of disulfide bond formation in mammals is important because of the involvement of protein misfolding in conditions such as diabetes, arthritis, cancer, and aging. However, the crystal structure of the enzyme is not available yet, which seriously hinders the understanding of biological function of Ero1-L{alpha}. Based on the crystal structure of yeast Ero1p, a rational three-dimensional structural model of Ero1-L{alpha} was built and the characteristics of the enzyme were hence investigated. The characteristic similarities and differences between Ero1-L{alpha} and Ero1p were compared on the basis of computational and experimental results, providing the first insight into the structure-function relationships of the enzymes. Both calculation and experiment got the concordant conclusion that FAD binds more tightly with Ero1-L{alpha} than Ero1p. In addition, the probable electron transfer pathway was proposed on the basis of the structural models.
- OSTI ID:
- 22199888
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 389, Issue 4; Other Information: Copyright (c) 2009 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
Similar Records
Structure and Mechanism of a Eukaryotic FMN Adenylyltransferase
Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum. Delta. H