PMID:9268657
| Citation |
Edwards, KJ, Ollis, DL and Dixon, NE (1997) Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: evidence for decreased mobility of loops upon complexation. J. Mol. Biol. 271:258-65 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1006/jmbi.1997.1151 |
| Keywords |
Amino Acid Isomerases/biosynthesis; Amino Acid Isomerases/chemistry; Amino Acid Isomerases/isolation & purification; Binding Sites; Carrier Proteins/biosynthesis; Carrier Proteins/chemistry; Carrier Proteins/isolation & purification; Computer Simulation; Crystallography, X-Ray; Cytoplasm/enzymology; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Hydrogen Bonding; Models, Molecular; Models, Structural; Peptidylprolyl Isomerase; Polymerase Chain Reaction; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification; Thermodynamics |
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