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PDBsum entry 1c5f

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protein Protein-protein interface(s) links
Isomerase/immunosuppressant PDB id
1c5f
Jmol
Contents
Protein chains
(+ 2 more) 177 a.a. *
(+ 2 more) 11 a.a. *
Waters ×337
* Residue conservation analysis
PDB id:
1c5f
Name: Isomerase/immunosuppressant
Title: Crystal structure of the cyclophilin-like domain from brugia complexed with cyclosporin a
Structure: Peptidyl-prolyl cis-trans isomerase 1. Chain: a, c, e, g, i, k, m, o. Fragment: cyclophilin-like domain, residues 1-177. Synonym: ppiase 1, rotamase, cyclophilin. Engineered: yes. Cyclosporin a. Chain: b, d, f, h, j, l, n, p. Synonym: cyclosporine, ciclosporin, ciclosporine. Engineered: yes
Source: Brugia malayi. Organism_taxid: 6279. Atcc: 75593. Gene: bmcyp-1. Expressed in: escherichia coli. Expression_system_taxid: 562. Ampr). Synthetic: yes. Tolypocladium inflatum.
Biol. unit: Tetramer (from PQS)
Resolution:
2.47Å     R-factor:   0.201     R-free:   0.249
Authors: P.J.Ellis,C.K.S.Carlow,D.Ma,P.Kuhn
Key ref:
P.J.Ellis et al. (2000). Crystal structure of the complex of brugia malayi cyclophilin and cyclosporin A. Biochemistry, 39, 592-598. PubMed id: 10642184 DOI: 10.1021/bi991730q
Date:
22-Nov-99     Release date:   03-Dec-99    
Supersedes: 1qtl
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q27450  (CYP1_BRUMA) -  Peptidyl-prolyl cis-trans isomerase 1
Seq:
Struc:
 
Seq:
Struc:
843 a.a.
177 a.a.
Protein chains
No UniProt id for this chain
Struc: 11 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, C, E, G, I, K, M, O: 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: 10.1021/bi991730q Biochemistry 39:592-598 (2000)
PubMed id: 10642184  
 
 
Crystal structure of the complex of brugia malayi cyclophilin and cyclosporin A.
P.J.Ellis, C.K.Carlow, D.Ma, P.Kuhn.
 
  ABSTRACT  
 
The resistance of the human parasite Brugia malayi to the antiparasitic activity of cyclosporin A (CsA) may arise from the presence of cyclophilins with relatively low affinity for the drug. The structure of the complex of B. malayi cyclophilin (BmCYP-1) and CsA, with eight independent copies in the asymmetric unit, has been determined at a resolution of 2.7 A. The low affinity of BmCYP-1 for CsA arises from incomplete preorganization of the binding site so that the formation of a hydrogen bond between His132 of BmCYP-1 and N-methylleucine 9 of CsA is associated with a shift in the backbone of approximately 1 A in this region.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
17429972 J.P.Collman, R.A.Decréau, Y.Yan, J.Yoon, and E.I.Solomon (2007).
Intramolecular single-turnover reaction in a cytochrome C oxidase model bearing a Tyr244 mimic.
  J Am Chem Soc, 129, 5794-5795.  
  17277440 V.Venugopal, B.Sen, A.K.Datta, and R.Banerjee (2007).
Structure of cyclophilin from Leishmania donovani at 1.97 A resolution.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 60-64.
PDB code: 2haq
  16510998 H.Hu, C.Q.Huang, H.L.Liu, Y.Han, L.Yu, and R.C.Bi (2005).
Crystallization and preliminary X-ray crystallographic studies of human cyclophilin J.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 216-218.  
11847225 D.Ma, L.S.Nelson, K.LeCoz, C.Poole, and C.K.Carlow (2002).
A novel cyclophilin from parasitic and free-living nematodes with a unique substrate- and drug-binding domain.
  J Biol Chem, 277, 14925-14932.  
12154086 L.Cavarec, T.Kamphausen, B.Dubourg, I.Callebaut, F.Lemeunier, D.Métivier, J.Feunteun, G.Fischer, and N.Modjtahedi (2002).
Identification and characterization of Moca-cyp. A Drosophila melanogaster nuclear cyclophilin.
  J Biol Chem, 277, 41171-41182.  
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. Where a reference describes a PDB structure, the PDB code is shown on the right.