PDBsum entry 2jzv

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protein links
Isomerase PDB id
Protein chain
111 a.a. *
* Residue conservation analysis
PDB id:
Name: Isomerase
Title: Solution structure of s. Aureus prsa-ppiase
Structure: Foldase protein prsa. Chain: a. Fragment: unp residues 140-245. Engineered: yes
Source: Staphylococcus aureus. Organism_taxid: 1280. Strain: atcc 292b. Gene: prsa. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 25 models
Authors: R.Seppala,H.Tossavainen,S.Heikkinen,H.Koskela,V.Kontinen, P.Permi
Key ref: O.Heikkinen et al. (2009). Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA--implications for the catalytic mechanism of parvulins. BMC Struct Biol, 9, 17. PubMed id: 19309529
21-Jan-08     Release date:   20-Jan-09    
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Protein chain
Pfam   ArchSchema ?
P60747  (PRSA_STAAM) -  Foldase protein PrsA
320 a.a.
111 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - 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!
  Biochemical function     isomerase activity     1 term  


    Added reference    
BMC Struct Biol 9:17 (2009)
PubMed id: 19309529  
Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA--implications for the catalytic mechanism of parvulins.
O.Heikkinen, R.Seppala, H.Tossavainen, S.Heikkinen, H.Koskela, P.Permi, I.Kilpeläinen.
BACKGROUND: Staphylococcus aureus is a Gram-positive pathogenic bacterium causing many kinds of infections from mild respiratory tract infections to life-threatening states as sepsis. Recent emergence of S. aureus strains resistant to numerous antibiotics has created a need for new antimicrobial agents and novel drug targets. S. aureus PrsA is a membrane associated extra-cytoplasmic lipoprotein which contains a parvulin-type peptidyl-prolyl cis-trans isomerase domain. PrsA is known to act as an essential folding factor for secreted proteins in Gram-positive bacteria and thus it is a potential target for antimicrobial drugs against S. aureus. RESULTS: We have solved a high-resolution solution structure of the parvulin-type peptidyl-prolyl cis-trans isomerase domain of S. aureus PrsA (PrsA-PPIase). The results of substrate peptide titrations pinpoint the active site and demonstrate the substrate preference of the enzyme. With detailed NMR spectroscopic investigation of the orientation and tautomeric state of the active site histidines we are able to give further insight into the structure of the catalytic site. NMR relaxation analysis gives information on the dynamic behaviour of PrsA-PPIase. CONCLUSION: Detailed structural description of the S. aureus PrsA-PPIase lays the foundation for structure-based design of enzyme inhibitors. The structure resembles hPin1-type parvulins both structurally and regarding substrate preference. Even though a wealth of structural data is available on parvulins, the catalytic mechanism has yet to be resolved. The structure of S. aureus PrsA-PPIase and our findings on the role of the conserved active site histidines help in designing further experiments to solve the detailed catalytic mechanism.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21138844 ..Jaremko, M.Jaremko, I.Elfaki, J.W.Mueller, A.Ejchart, P.Bayer, and I.Zhukov (2011).
Structure and dynamics of the first archaeal parvulin reveal a new functionally important loop in parvulin-type prolyl isomerases.
  J Biol Chem, 286, 6554-6565.
PDB code: 2rqs
20487272 H.L.Hyyryläinen, B.C.Marciniak, K.Dahncke, M.Pietiäinen, P.Courtin, M.Vitikainen, R.Seppala, A.Otto, D.Becher, M.P.Chapot-Chartier, O.P.Kuipers, and V.P.Kontinen (2010).
Penicillin-binding protein folding is dependent on the PrsA peptidyl-prolyl cis-trans isomerase in Bacillus subtilis.
  Mol Microbiol, 77, 108-127.  
  19866485 U.Weininger, R.P.Jakob, M.Kovermann, J.Balbach, and F.X.Schmid (2010).
The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity.
  Protein Sci, 19, 6.
PDB code: 2kgj
19664234 K.M.Rathbun, J.E.Hall, and S.A.Thompson (2009).
Cj0596 is a periplasmic peptidyl prolyl cis-trans isomerase involved in Campylobacter jejuni motility, invasion, and colonization.
  BMC Microbiol, 9, 160.  
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