2NUL

PEPTIDYLPROLYL ISOMERASE FROM E. COLI

Summary for 2NUL

• Entry DOI: 10.2210/pdb2nul/pdb
• Descriptor: PEPTIDYLPROLYL ISOMERASE (2 entities in total)
• Functional Keywords: isomerase, rotamase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P23869
• Total number of polymer chains: 1
• Total formula weight: 18174.45

Authors

Edwards, K.J.,Ollis, D.L. (deposition date: 1996-11-14, release date: 1997-11-19, Last modification date: 2024-05-22)

Primary citation

Edwards, K.J.,Ollis, D.L.,Dixon, N.E.
Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: evidence for decreased mobility of loops upon complexation.
J.Mol.Biol., 271:258-265, 1997

PubMed 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.

PubMed: 9268657
DOI: 10.1006/jmbi.1997.1151

Experimental method

X-RAY DIFFRACTION (2.1 Å)