PDBsum entry 3jym

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protein Protein-protein interface(s) links
Isomerase PDB id
Protein chains
301 a.a. *
* Residue conservation analysis
PDB id:
Name: Isomerase
Title: Crystal structure of the 3 fkbp domains of wheat fkbp73
Structure: Fk506-binding protein (fkbp) from wheat. Chain: a, b. Engineered: yes
Source: Triticum aestivum. Wheat. Organism_taxid: 4565. Expressed in: escherichia coli. Expression_system_taxid: 562
2.28Å     R-factor:   0.274     R-free:   0.343
Authors: O.Dym,A.Breiman,Israel Structural Proteomics Center (Ispc)
Key ref: T.Unger et al. (2010). Crystal structure of the three FK506 binding protein domains of wheat FKBP73: evidence for a unique wFK73_2 domain. J Struct Funct Genomics, 11, 113-123. PubMed id: 20306145
22-Sep-09     Release date:   16-Jun-10    
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Protein chains
Pfam   ArchSchema ?
Q43207  (FKB70_WHEAT) -  70 kDa peptidyl-prolyl isomerase
559 a.a.
301 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Peptidylprolyl isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Peptidylproline (omega=180) = peptidylproline (omega=0)
Peptidylproline (omega=180)
= peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     protein folding   1 term 


    Added reference    
J Struct Funct Genomics 11:113-123 (2010)
PubMed id: 20306145  
Crystal structure of the three FK506 binding protein domains of wheat FKBP73: evidence for a unique wFK73_2 domain.
T.Unger, O.Dym, S.Albeck, Y.Jacobovitch, R.Bernehim, D.Marom, O.Pisanty, A.Breiman.
Here we describe the crystal structure of the N-terminal domain of the FK506-binding protein (FKBP) from wheat (wFKBP73), which is the first structure presenting three FK domains (wFK73_1, wFK73_2 and wFK73_3). The crystal model includes wFK73_2 and wFK73_3 domains and only part of the wFK73_1 domain. The wFK73_1 domain is responsible for binding FK506 and for peptidyl prolyl cis/trans isomerase (PPIase) activity, while the wFK73_2 and wFK73_3 domains lack these activities. A structure-based sequence comparison demonstrated that the absence of a large enough hydrophobic pocket important for PPIase activity, and of the conserved residues necessary for drug binding in the wFK73_2 and wFK73_3 domains explains the lack of these activities in these domains. Sequence and structural comparison between the three wFKBP73 domains suggest that the wFK73_2 domain is the most divergent. A structural comparison of the FK domains of wFKBP73 with other FKBPs containing more than one FK domain, revealed that while the overall architecture of each of the three FK domains displays a typical FKBP fold, their relative arrangement in space is unique and may have important functional implications. We suggest that the existence of FKBPs with three FK domains offers additional interactive options for these plant proteins enlarging the overall regulatory functions of these proteins.