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 Cited by 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: 9268657DOI: 10.1006/jmbi.1997.1151 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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