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Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases

¹ Organische Chemie II, Department Chemie, Technische Universität (TU) München, D-85747, Garching, Germany
² Max-Planck-Forschungsstelle für Enzymologie der Proteinfaltung, D-06120 Halle (Saale), Germany

(RECEIVED March 24, 2004; FINAL REVISION May 7, 2004; ACCEPTED May 18, 2004)

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 / 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 Å 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 -sheet. The N terminus forms a -strand, followed by a large stretch comprising three -helices. A loop region containing a short -strand separates these helices from a fourth -helix. The C terminus consists of two more -strands completing the four-stranded anti-parallel -sheet with strand order 2143. Interestingly, the third -strand includes a Gly-Pro cis peptide bond. The curved -strand forms a hydrophobic binding pocket together with -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.

Keywords: protein structure; NMR; parvulin; PPIase; cis peptide bond

Abbreviations: ARIA, ambiguous restraints in iterative assignment • CNS, crystallography and NMR system • CSI, chemical shift index • DTE, dithioerythrol • EDTA, ethylendiamine tetraacetate • HSQC, heteronuclear single-quantum correlation • isopropyl ß-D-thiogalactopyranoside (IPTG) • MEXICO, measurement of exchange in isotopically labelled compounds • RMSD, root mean square deviation

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04756704.

Reprint requests to: Gerd Gemmecker, Department Chemie, OC II, TU München, Lichtenbergstr. 4, D-85747 Garching, Germany; e-mail: Gerd.Gemmecker{at}ch.tum.de; fax: +49 (89) 289 13210.

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