Caenopore-5: the three-dimensional structure of an antimicrobial protein from Caenorhabditis elegans.
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.
Mysliwy
Justyna
J
Institute of Biochemistry, Christian-Albrechts-University Kiel, Olshausenstr. 40, 24098 Kiel, Germany.
Dingley
Andrew J
AJ
Stanisak
Mareike
M
Jung
Sascha
S
Lorenzen
Inken
I
Roeder
Thomas
T
Leippe
Matthias
M
Grötzinger
Joachim
J
D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000737:chemistry* / Q000276:immunology; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry* / Q000276:immunology; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D020033:Protein Isoforms / Q000737:chemistry; D020836:Protein Structure, Quaternary; D020539:Sequence Analysis, Protein
D029742:Caenorhabditis elegans Proteins; D020033:Protein Isoforms