PDBsum entry 2js9

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protein links
Antimicrobial protein PDB id
Jmol PyMol
Protein chain
81 a.a. *
* Residue conservation analysis
PDB id:
Name: Antimicrobial protein
Title: Structure of caenopore-5 (81 pro cis conformer)
Structure: Saposin-like protein family protein 5. Chain: a. Engineered: yes
Source: Caenorhabditis elegans. Organism_taxid: 6239. Gene: spp-5. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 15 models
Authors: J.Mysliwy,J.Grotzinger
Key ref: J.Mysliwy et al. (2010). Caenopore-5: the three-dimensional structure of an antimicrobial protein from Caenorhabditis elegans. Dev Comp Immunol, 34, 323-330. PubMed id: 19917307
02-Jul-07     Release date:   14-Oct-08    
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Protein chain
Pfam   ArchSchema ?
Q86FL8  (Q86FL8_CAEEL) -  SaPosin-like Protein family
103 a.a.
81 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     transmembrane transport   3 terms 
  Biochemical function     channel activity     1 term  


Dev Comp Immunol 34:323-330 (2010)
PubMed id: 19917307  
Caenopore-5: the three-dimensional structure of an antimicrobial protein from Caenorhabditis elegans.
J.Mysliwy, A.J.Dingley, M.Stanisak, S.Jung, I.Lorenzen, T.Roeder, M.Leippe, J.Grötzinger.
The caenopore-5 protein encoded by the spp-5 gene is one of the 33 caenopores identified in Caenorhabditis elegans and is a pore-forming peptide which plays an important role in the elimination of Escherichia coli ingested by the worm. Thus, caenopore-5 appears to contribute to the nutrition of the worm while simultaneously protecting the organism against pathogens. Here, three-dimensional heteronuclear NMR spectroscopy was used to solve the solution structure of caenopore-5. The NMR data revealed that two conformers of caenopore-5 exist in solution which differ by the isomerization of the peptide bond of Pro-81. The overall structure of the two caenopore-5 conformers consists of five amphiphatic helices connected by three disulfide bonds. The five helices are arranged in a folded leaf which is the characteristic signature of the SAPLIP family. The structure presented here is the first of an effector protein of the defensive system elucidated for the well-known model organism C. elegans.