1ZK6

NMR solution structure of B. subtilis PrsA PPIase


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 30 
  • Conformers Submitted: 15 
  • Selection Criteria: structures with the least restraint violations, structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein from Bacillus subtilis

Tossavainen, H.Permi, P.Purhonen, S.L.Sarvas, M.Kilpelainen, I.Seppala, R.

(2006) FEBS Lett 580: 1822-1826

  • DOI: https://doi.org/10.1016/j.febslet.2006.02.042
  • Primary Citation of Related Structures:  
    1ZK6

  • PubMed Abstract: 

    PrsA is a peptidyl-prolyl isomerase (PPIase) from Bacillus subtilis belonging to the parvulin family of PPIases. It is a membrane bound lipoprotein at the membrane-wall interface, involved in folding of exported proteins. We present the NMR solution structure of the PPIase domain of PrsA, the first from a Gram-positive bacterium. In addition we mapped out the active site with NMR titration experiments. A high degree of conservation with other members of the parvulin family was revealed in the structure and binding site. Interactions with substrate peptides were also characterized by mutated domains revealing that H122 is indispensable for overall correct folding.


  • Organizational Affiliation

    NMR Laboratory, Institute of Biotechnology, Viikinkaari 1, P.O. Box 65, FI-00014, University of Helsinki, Helsinki, Finland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Foldase protein prsA93Bacillus subtilisMutation(s): 0 
Gene Names: prsA
EC: 5.2.1.8
UniProt
Find proteins for P24327 (Bacillus subtilis (strain 168))
Explore P24327 
Go to UniProtKB:  P24327
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP24327
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 30 
  • Conformers Submitted: 15 
  • Selection Criteria: structures with the least restraint violations, structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-03-28
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Data collection, Database references, Derived calculations
  • Version 1.4: 2024-05-22
    Changes: Data collection