PDBsum entry: 1fjd

Isomerase

PDB id: 1fjd

Contents

Protein chain

104 a.a. *

* Residue conservation analysis

PDB id:

1fjd

Name:

Isomerase

Title:

Human parvulin-like peptidyl prolyl cis/trans isomerase, hpar14

Structure:

Peptidyl prolyl cis/trans isomerase (ppiase). Chain: a. Fragment: residues 28-131. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Organ: lung. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

T.Terada,M.Shirouzu,Y.Fukumori,F.Fujimori,Y.Ito,T.Kigawa, S.Yokoyama,T.Uchida,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

T.Terada et al. (2001). Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14. J Mol Biol, 305, 917-926. PubMed id: 11162102 DOI: 10.1006/jmbi.2000.4293

Date:

08-Aug-00 Release date: 08-Aug-01

Protein chain

Q9Y237  (PIN4_HUMAN) -  Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4

Seq: 131 a.a.

Struc: 104 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.5.2.1.8 - Peptidylprolyl isomerase.
• Reaction: Peptidylproline (omega=180) = peptidylproline (omega=0)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biochemical function: isomerase activity (1 term)

Added reference

DOI no: 10.1006/jmbi.2000.4293

J Mol Biol 305:917-926 (2001)

PubMed id: 11162102

Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14.

T.Terada, M.Shirouzu, Y.Fukumori, F.Fujimori, Y.Ito, T.Kigawa, S.Yokoyama, T.Uchida.

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.

Selected figure(s)

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.

Figures were selected by an automated process.