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PDBsum entry 1w74

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protein Protein-protein interface(s) links
Isomerase PDB id
1w74
Jmol
Contents
Protein chains
171 a.a. *
Waters ×13
* Residue conservation analysis
PDB id:
1w74
Name: Isomerase
Title: X-ray structure of peptidyl-prolyl cis-trans isomerase a, ppia, rv0009, from mycobacterium tuberculosis.
Structure: Peptidyl-prolyl cis-trans isomerase a. Chain: a, b. Synonym: ppiase a, rotamase a. Engineered: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
2.6Å     R-factor:   0.213     R-free:   0.229
Authors: L.M.Henriksson,P.Johansson,T.Unge,S.L.Mowbray
Key ref:
L.M.Henriksson et al. (2004). X-ray structure of peptidyl-prolyl cis-trans isomerase A from Mycobacterium tuberculosis. Eur J Biochem, 271, 4107-4113. PubMed id: 15479239 DOI: 10.1111/j.1432-1033.2004.04348.x
Date:
27-Aug-04     Release date:   20-Oct-04    
PROCHECK
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 Headers
 References

Protein chains
Pfam  
P9WHW2  (PPIA_MYCTO) -  Peptidyl-prolyl cis-trans isomerase A
Seq:
Struc:
182 a.a.
171 a.a.
Protein chains
Pfam  
P9WHW3  (PPIA_MYCTU) -  Peptidyl-prolyl cis-trans isomerase A
Seq:
Struc:
182 a.a.
171 a.a.
Key:    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!
  Cellular component     cytoplasm   1 term 
  Biological process     protein folding   2 terms 
  Biochemical function     isomerase activity     2 terms  

 

 
    Added reference    
 
 
DOI no: 10.1111/j.1432-1033.2004.04348.x Eur J Biochem 271:4107-4113 (2004)
PubMed id: 15479239  
 
 
X-ray structure of peptidyl-prolyl cis-trans isomerase A from Mycobacterium tuberculosis.
L.M.Henriksson, P.Johansson, T.Unge, S.L.Mowbray.
 
  ABSTRACT  
 
Peptidyl-prolyl cis-trans isomerases (EC 5.2.1.8) catalyse the interconversion of cis and trans peptide bonds and are therefore considered to be important for protein folding. They are also thought to participate in processes such as signalling, cell surface recognition, chaperoning and heat-shock response. Here we report the soluble expression of recombinant Mycobacterium tuberculosis peptidyl-prolyl cis-trans isomerase PpiA in Escherichia coli, together with an investigation of its structure and biochemical properties. The protein was shown to be active in a spectrophotometric assay, with an estimated kcat/Km of 2.0 x 10(6) m(-1).s(-1). The X-ray structure of PpiA was solved by molecular replacement, and refined to a resolution of 2.6 A with R and Rfree values of 21.3% and 22.9%, respectively. Comparisons to known structures show that the PpiA represents a slight variation on the peptidyl-prolyl cis-trans isomerase fold, previously not represented in the Protein Data Bank. Inspection of the active site suggests that specificity for substrates and cyclosporin A will be similar to that found for most other enzymes of this structural family. Comparison to the sequence of the second M. tuberculosis enzyme, PpiB, suggests that binding of peptide substrates as well as cyclosporin A may differ in that case.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Pseudo translation. A large nonorigin peak was found in the native Patterson map (contoured at 1.5 with intervals of 0.5 , where = 0.32 e·Å^–3), indicating the pure translation between the two molecules in the asymmetric unit.
Figure 3.
Fig. 3. Structure of MtPpiA.(A) The overall structure of MtPpiA is illustrated in a ribbon drawing. The chain is coloured beginning with blue at the N-terminus going through the rainbow to red at the C terminus. (B) Stereo view of the A molecule's active site with refined |2F[o]-F[c]| map contoured at 1 . For clarity, electron density for the protein alone is shown in this panel. (C) Stereo view of the active site showing only density attributable to partially occupied peptide. The expected site for binding the peptide HAGPIA was determined using a superposition of the human enzyme complex in PDB entry 1AWQ [14]. The superimposed peptide is shown in magenta. The |2F[o]-F[c]| map was then contoured at 0.8 in that region. Active site residues are labelled in black.
 
  The above figures are reprinted by permission from the Federation of European Biochemical Societies: Eur J Biochem (2004, 271, 4107-4113) copyright 2004.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20038535 G.M.Scandurra, G.W.de Lisle, S.M.Cavaignac, M.Young, R.P.Kawakami, and D.M.Collins (2010).
Assessment of live candidate vaccines for paratuberculosis in animal models and macrophages.
  Infect Immun, 78, 1383-1389.  
17103061 A.Manteca, A.I.Pelaez, R.Zardoya, and J.Sanchez (2006).
Actinobacteria cyclophilins: phylogenetic relationships and description of new class- and order-specific paralogues.
  J Mol Evol, 63, 719-732.  
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