spacer
spacer

PDBsum entry 1a33

Go to PDB code: 
protein links
Isomerase PDB id
1a33
Jmol
Contents
Protein chain
174 a.a. *
Waters ×234
* Residue conservation analysis
PDB id:
1a33
Name: Isomerase
Title: Peptidylprolyl isomerase, cyclophilin-like domain from brugia malayi
Structure: Peptidylprolyl isomerase. Chain: a. Fragment: cyclophilin-like domain. Engineered: yes
Source: Brugia malayi. Organism_taxid: 6279. Atcc: atcc 75593. Collection: atcc 75593. Gene: bmcyp-1. Expressed in: escherichia coli. Expression_system_taxid: 562. Pmb1 and ampr).
Resolution:
2.15Å     R-factor:   0.169     R-free:   0.211
Authors: V.Mikol,D.Ma,C.K.S.Carlow
Key ref:
V.Mikol et al. (1998). Crystal structure of the cyclophilin-like domain from the parasitic nematode Brugia malayi. Protein Sci, 7, 1310-1316. PubMed id: 9655334 DOI: 10.1002/pro.5560070606
Date:
27-Jan-98     Release date:   29-Jul-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q27450  (CYP1_BRUMA) -  Peptidyl-prolyl cis-trans isomerase 1
Seq:
Struc:
 
Seq:
Struc:
843 a.a.
174 a.a.
Key:    PfamA domain  PfamB 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    
 
 
DOI no: 10.1002/pro.5560070606 Protein Sci 7:1310-1316 (1998)
PubMed id: 9655334  
 
 
Crystal structure of the cyclophilin-like domain from the parasitic nematode Brugia malayi.
V.Mikol, D.Ma, C.K.Carlow.
 
  ABSTRACT  
 
Cyclophilins are a family of proteins that exhibit peptidyl-prolyl cis-trans isomerase activity and bind the immunosuppressive agent cyclosporin A (CsA). Brugia malayi is a filarial nematode parasite of humans, for which a cyclophilin-like domain was identified at the N-terminal of a protein containing 843 amino acid residues. There are two differences in sequence in the highly conserved CsA binding site: A histidine and a lysine replace a tryptophan and an alanine, respectively. The crystal structure of this domain has been determined by the molecular replacement method and refined to an R-factor of 16.9% at 2.15 A resolution. The overall structure is similar to other cyclophilins; however, major differences occur in two loops. Comparison of the CsA binding site of this domain with members of the cyclophilin family shows significant structural differences, which can account for the reduced sensitivity of the Brugia malayi protein to inhibition by CsA.
 
  Selected figure(s)  
 
Figure 1.
Fig. 1. Schematic representation f CypBm- I. All representing molecules were prepared with the program MOLSCRIPT Kraulis. 1991 ).
Figure 3.
Fig. 3. Stereopicture of the overlay of CypBm-1 on CypHA(a) and onCypHB(b).The C" trace of CypBm-l (continuous lines) is superimposed on that of CypHA(broken lines) (A) andon that o CypHB lines) B). Some residues of CypBm-1 are labeled.
 
  The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (1998, 7, 1310-1316) copyright 1998.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
17225137 P.Mark, and L.Nilsson (2007).
A molecular dynamics study of Cyclophilin A free and in complex with the Ala-Pro dipeptide.
  Eur Biophys J, 36, 213-224.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.