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Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: Evidence for decreased mobility of loops upon complexation

Journal Article


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 Å resolution. The enzyme crystallized in the orthorhombic C2221 space group with unit cell dimensions of n = 44.7 Å, b = 68.2 Å and c = 102.0 Å. 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.

Publication Date


  • 1997

Citation


  • Edwards, K. J., Ollis, D. L., & Dixon, N. E. (1997). Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: Evidence for decreased mobility of loops upon complexation. Journal of Molecular Biology, 271(2), 258-265. doi:10.1006/jmbi.1997.1151

Scopus Eid


  • 2-s2.0-0031571592

Start Page


  • 258

End Page


  • 265

Volume


  • 271

Issue


  • 2

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 Å resolution. The enzyme crystallized in the orthorhombic C2221 space group with unit cell dimensions of n = 44.7 Å, b = 68.2 Å and c = 102.0 Å. 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.

Publication Date


  • 1997

Citation


  • Edwards, K. J., Ollis, D. L., & Dixon, N. E. (1997). Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: Evidence for decreased mobility of loops upon complexation. Journal of Molecular Biology, 271(2), 258-265. doi:10.1006/jmbi.1997.1151

Scopus Eid


  • 2-s2.0-0031571592

Start Page


  • 258

End Page


  • 265

Volume


  • 271

Issue


  • 2