| Autor: |
Edwards, Karen J., Ollis, David L., Dixon, Nicholas E. |
| Zdroj: |
JMB Online (Journal of Molecular Biology); August 15, 1997, Vol. 271 Issue: 2 p258-265, 8p |
| Abstrakt: |
The structure of the unliganded form of the Escherichia coli cytoplasmic peptidyl-prolyl isomerase (ppiB gene product) in a new crystal form was determined by the molecular replacement method and refined to an R-factor of 16.1% at 2.1 A˚ resolution. The enzyme crystallized in the orthorhombic C2221 space group with unit cell dimensions of a = 44.7 A˚, b = 68.2 A˚ and c = 102.0 A˚. Comparison with the reported structure of the enzyme complexed with the tripeptide substrate succinyl-Ala-Pro-Ala-p-nitroanilide revealed subtle changes that occur upon complex formation. There is evidence to suggest that two surface loops have significantly reduced mobility in the complexed structure. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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