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PDBsum entry 3ey6

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protein links
Isomerase PDB id
3ey6
Jmol
Contents
Protein chain
118 a.a. *
Waters ×244
* Residue conservation analysis
PDB id:
3ey6
Name: Isomerase
Title: Crystal structure of the fk506-binding domain of human fkbp3
Structure: Fk506-binding protein 8. Chain: a. Fragment: fk506 binding domain. Synonym: peptidyl-prolyl cis-trans isomerase, ppiase, rotam kda fk506-binding protein, hfkbp38, fkbpr38. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: fkbp38, fkbp8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.05Å     R-factor:   0.136     R-free:   0.161
Authors: C.Parthier,M.Maestre-Martinez,P.Neumann,F.Edlich,G.Fischer,C M.T.Stubbs
Key ref: M.Maestre-Martínez et al. (2011). A charge-sensitive loop in the FKBP38 catalytic domain modulates Bcl-2 binding. J Mol Recognit, 24, 23-34. PubMed id: 20140889
Date:
19-Oct-08     Release date:   27-Oct-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q14318  (FKBP8_HUMAN) -  Peptidyl-prolyl cis-trans isomerase FKBP8
Seq:
Struc:
412 a.a.
118 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.5.2.1.8  - 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 Mol Recognit 24:23-34 (2011)
PubMed id: 20140889  
 
 
A charge-sensitive loop in the FKBP38 catalytic domain modulates Bcl-2 binding.
M.Maestre-Martínez, K.Haupt, F.Edlich, P.Neumann, C.Parthier, M.T.Stubbs, G.Fischer, C.Lücke.
 
  ABSTRACT  
 
The Bcl-2 inhibitor FKBP38 is regulated by the Ca(2+)-sensor calmodulin (CaM). Here we show a hitherto unknown low-affinity cation-binding site in the FKBP domain of FKBP38, which may afford an additional level of regulation based on electrostatic interactions. Fluorescence titration experiments indicate that in particular the physiologically relevant Ca(2+) ion binds to this site. NMR-based chemical shift perturbation data locate this cation-interaction site within the beta5-alpha1 loop (Leu90-Ile96) of the FKBP domain, which contains the acidic Asp92 and Asp94 side-chains. Binding constants were subsequently determined for K(+), Mg(2+), Ca(2+), and La(3+), indicating that the net charge and the radius of the ion influences the binding interaction. X-ray diffraction data furthermore show that the conformation of the beta5-alpha1 loop is influenced by the presence of a positively charged guanidinium group belonging to a neighboring FKBP38 molecule in the crystal lattice. The position of the cation-binding site has been further elucidated based on pseudocontact shift data obtained by NMR via titration with Tb(3+). Elimination of the Ca(2+)-binding capacity by substitution of the respective aspartate residues in a D92N/D94N double-substituted variant reduces the Bcl-2 affinity of the FKBP38(35-153)/CaM complex to the same degree as the presence of Ca(2+) in the wild-type protein. Hence, this charge-sensitive site in the FKBP domain participates in the regulation of FKBP38 function by enabling electrostatic interactions with ligand proteins and/or salt ions such as Ca(2+). Copyright (c) 2010 John Wiley & Sons, Ltd.