1JNS

NMR Structure of the E. coli Peptidyl-Prolyl cis/trans-Isomerase Parvulin 10

Summary for 1JNS

• Entry DOI: 10.2210/pdb1jns/pdb
• Related: 1JNT
• NMR Information: BMRB: 5225
• Descriptor: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE C (1 entity in total)
• Functional Keywords: alpha-beta sandwich, cis peptide bond, isomerase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A9L5
• Total number of polymer chains: 1
• Total formula weight: 10117.84

Authors

Kuehlewein, A.,Voll, G.,Schelbert, B.,Kessler, H.,Fischer, G.,Rahfeld, J.U.,Gemmecker, G. (deposition date: 2001-07-25, release date: 2003-06-17, Last modification date: 2024-05-22)

Primary citation

Kuehlewein, A.,Voll, G.,Alvarez, B.H.,Kessler, H.,Fischer, G.,Rahfeld, J.U.,Gemmecker, G.
Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases.
Protein Sci., 13:2378-2387, 2004

PubMed Abstract: E. coli Par10 is a peptidyl-prolyl cis/trans isomerase (PPIase) from Escherichia coli catalyzing the isomerization of Xaa-Pro bonds in oligopeptides with a broad substrate specificity. The structure of E. coli Par10 has been determined by multidimensional solution-state NMR spectroscopy based on 1207 conformational constraints (1067 NOE-derived distances, 42 vicinal coupling-constant restraints, 30 hydrogen-bond restraints, and 68 phi/psi restraints derived from the Chemical Shift Index). Simulated-annealing calculations with the program ARIA and subsequent refinement with XPLOR yielded a set of 18 convergent structures with an average backbone RMSD from mean atomic coordinates of 0.50 A within the well-defined secondary structure elements. E. coli Par10 is the smallest known PPIase so far, with a high catalytic efficiency comparable to that of FKBPs and cyclophilins. The secondary structure of E. coli Par10 consists of four helical regions and a four-stranded antiparallel beta-sheet. The N terminus forms a beta-strand, followed by a large stretch comprising three alpha-helices. A loop region containing a short beta-strand separates these helices from a fourth alpha-helix. The C terminus consists of two more beta-strands completing the four-stranded anti-parallel beta-sheet with strand order 2143. Interestingly, the third beta-strand includes a Gly-Pro cis peptide bond. The curved beta-strand forms a hydrophobic binding pocket together with alpha-helix 4, which also contains a number of highly conserved residues. The three-dimensional structure of Par10 closely resembles that of the human proteins hPin1 and hPar14 and the plant protein Pin1At, belonging to the same family of highly homologous proteins.

PubMed: 15322281
DOI: 10.1110/ps.04756704

Experimental method

SOLUTION NMR