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PDBsum entry 1fjd

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Isomerase PDB id
1fjd
Jmol
Contents
Protein chain
104 a.a. *
* Residue conservation analysis

References listed in PDB file
Key reference
Title Solution structure of the human parvulin-Like peptidyl prolyl cis/trans isomerase, Hpar14.
Authors T.Terada, M.Shirouzu, Y.Fukumori, F.Fujimori, Y.Ito, T.Kigawa, S.Yokoyama, T.Uchida.
Ref. J Mol Biol, 2001, 305, 917-926. [DOI no: 10.1006/jmbi.2000.4293]
PubMed id 11162102
Abstract
The hPar14 protein is a peptidyl prolyl cis/trans isomerase and is a human parvulin homologue. The hPar14 protein shows about 30 % sequence identity with the other human parvulin homologue, hPin1. Here, the solution structure of hPar14 was determined by nuclear magnetic resonance spectroscopy. The N-terminal 35 residues preceding the peptidyl prolyl isomerase domain of hPar14 are unstructured, whereas hPin1 possesses the WW domain at its N terminus. The fold of residues 36-131 of hPar14, which comprises a four-stranded beta-sheet and three alpha-helices, is superimposable onto that of the peptidyl prolyl isomerase domain of hPin1. To investigate the interaction of hPar14 with a substrate, the backbone chemical-shift changes of hPar14 were monitored during titration with a tetra peptide. Met90, Val91, and Phe94 around the N terminus of alpha3 showed large chemical-shift changes. These residues form a hydrophobic patch on the molecular surface of hPar14. Two of these residues are conserved and have been shown to interact with the proline residue of the substrate in hPin1. On the other hand, hPar14 lacks the hPin1 positively charged residues (Lys63, Arg68, and Arg69), which determine the substrate specificity of hPin1 by interacting with phosphorylated Ser or Thr preceding the substrate Pro, and exhibits a different structure in the corresponding region. Therefore, the mechanism determining the substrate specificity seems to be different between hPar14 and hPin1.
Figure 3.
Figure 3. (a) A stereo view of the superimposition of the backbone (N, C^a, and CO) traces of the 19 NMR-derived structures of hPar14; residues 36-131 are shown. (b) Ribbon representation of the minimized average structure of hPar14 (resides 36-131).
Figure 5.
Figure 5. (a) Ribbon representation of the minimized average structure of hPar14 (residues 36-131) and (b) its right side view. The atoms of Lys47, Lys50, and Lys119 are represented by a space-filling model, and are colored cyan. (c) Ribbon representation of the PPIase domain of hPin1 (residues 53-163) and (d) its right side view. The atoms of Lys63, Arg68, and Arg69 are represented by a space-filling model, and are colored cyan. The Ala-Pro dipeptide and the sulfate ion are also shown as a space-filling model, and are colored yellow.
The above figures are reprinted by permission from Elsevier: J Mol Biol (2001, 305, 917-926) copyright 2001.
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