Annular Arrangement and Collaborative Actions of Four Domains of Protein-disulfide Isomerase
| Autor: | Chih-chen Wang, Hui Li, Sheng-jian Li, Yuan-yuan Shi, Xin-guo Hong |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
inorganic chemicals
Molecular mass Small-angle X-ray scattering Scattering Dimer Cell Biology Nuclear magnetic resonance spectroscopy Isomerase Biochemistry nervous system diseases body regions chemistry.chemical_compound Crystallography Monomer chemistry Protein disulfide-isomerase Molecular Biology |
| Zdroj: | Journal of Biological Chemistry. 281:6581-6588 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m508422200 |
| Popis: | We presented for the first time a small angle x-ray scattering study of intact protein-disulfide isomerase (PDI) in solution. The restored model revealed that PDI is a short and roughly elliptical cylinder with a molecular mass of 69 kDa and dimensions of 105 x 65 x 40 A, and the four thioredoxin-fold domains in the order a-b-b'-a' are arranged in an annular fashion. Atomic force microscope imaging also supported the finding that PDI appears as an approximately flat elliptical cylinder. A PDI species with apparent molecular mass of 116 kDa measured by using size-exclusion chromatography, previously assumed to be a dimer, was determined to exist mainly as a monomer by using analytical ultracentrifugation. The C-terminal fragment 441-491 contributed to the anomalous molecular mass determination of PDI by size-exclusion chromatography. The annular model of PDI accounted for the cooperative properties of the four domains in both the isomerase and chaperone functions of PDI. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|