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1jns

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{{STRUCTURE_1jns| PDB=1jns | SCENE= }}
{{STRUCTURE_1jns| PDB=1jns | SCENE= }}
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'''NMR Structure of the E. coli Peptidyl-Prolyl cis/trans-Isomerase Parvulin 10'''
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===NMR Structure of the E. coli Peptidyl-Prolyl cis/trans-Isomerase Parvulin 10===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15322281 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15322281}}
==About this Structure==
==About this Structure==
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1JNS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JNS OCA].
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1JNS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JNS OCA].
==Reference==
==Reference==
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[[Category: Alpha-beta sandwich]]
[[Category: Alpha-beta sandwich]]
[[Category: Cis peptide bond]]
[[Category: Cis peptide bond]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:28:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:31:32 2008''

Revision as of 17:31, 1 July 2008

Image:1jns.png

Template:STRUCTURE 1jns

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

Template:ABSTRACT PUBMED 15322281

About this Structure

1JNS is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases., Kuhlewein A, Voll G, Hernandez Alvarez B, Kessler H, Fischer G, Rahfeld JU, Gemmecker G, Protein Sci. 2004 Sep;13(9):2378-87. PMID:15322281

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