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PDBsum entry 2a2n

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protein ligands Protein-protein interface(s) links
Isomerase PDB id
2a2n
Jmol
Contents
Protein chains
164 a.a. *
Ligands
GOL
Waters ×388
* Residue conservation analysis
PDB id:
2a2n
Name: Isomerase
Title: Crystal structure of the peptidylprolyl isomerase domain of ppwd1
Structure: Peptidylprolyl isomerase domain and wd repeat con chain: a, b, c. Fragment: peptidylprolyl isomerase domain, residues 482-646 engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ppwd1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.65Å     R-factor:   0.202     R-free:   0.245
Authors: J.R.Walker,T.L.Davis,E.M.Newman,F.Mackenzie,M.Sundstrom,C.Ar A.Edwards,A.Bochkarev,S.Dhe-Paganon,Structural Genomics Con (Sgc)
Key ref: T.L.Davis et al. (2008). The crystal structure of human WD40 repeat-containing peptidylprolyl isomerase (PPWD1). FEBS J, 275, 2283-2295. PubMed id: 18397323
Date:
22-Jun-05     Release date:   05-Jul-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q96BP3  (PPWD1_HUMAN) -  Peptidylprolyl isomerase domain and WD repeat-containing protein 1
Seq:
Struc:
 
Seq:
Struc:
646 a.a.
164 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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   2 terms 
  Biochemical function     peptidyl-prolyl cis-trans isomerase activity     1 term  

 

 
    Added reference    
 
 
FEBS J 275:2283-2295 (2008)
PubMed id: 18397323  
 
 
The crystal structure of human WD40 repeat-containing peptidylprolyl isomerase (PPWD1).
T.L.Davis, J.R.Walker, H.Ouyang, F.MacKenzie, C.Butler-Cole, E.M.Newman, E.Z.Eisenmesser, S.Dhe-Paganon.
 
  ABSTRACT  
 
Cyclophilins comprise one of the three classes of peptidylprolyl isomerases found in all eukaryotic and prokaryotic organisms, as well as viruses. Many of the 17 annotated human cyclophilins contain the catalytic domain in tandem with other domains, and many of the specific functions of a particular cyclophilin or its associated domains remain unknown. The structure of the isomerase domain from a spliceosome-associated cyclophilin, PPWD1 (peptidylprolyl isomerase containing WD40 repeat), has been solved to 1.65 A. In the crystal, the N-terminus of one isomerase domain is bound in the active site of a neighboring isomerase molecule in a manner analogous to substrate. NMR solution studies show that this sequence binds to the active site of the cyclophilin, but cannot be turned over by the enzyme. A pseudo-substrate immediately N-terminal to the cyclophilin domain in PPWD1 could have wider implications for the function of this cyclophilin in the spliceosome, where it is located in human cells.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20602248 A.Galat, and J.Bua (2010).
Molecular aspects of cyclophilins mediating therapeutic actions of their ligands.
  Cell Mol Life Sci, 67, 3467-3488.  
20676357 T.L.Davis, J.R.Walker, V.Campagna-Slater, P.J.Finerty, R.Paramanathan, G.Bernstein, F.MacKenzie, W.Tempel, H.Ouyang, W.H.Lee, E.Z.Eisenmesser, and S.Dhe-Paganon (2010).
Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases.
  PLoS Biol, 8, e1000439.  
19555495 J.Krücken, G.Greif, and G.von Samson-Himmelstjerna (2009).
In silico analysis of the cyclophilin repertoire of apicomplexan parasites.
  Parasit Vectors, 2, 27.  
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