2JSA

Solution structure of Caenopore-5 (81 Pro Trans confomer)

Summary for 2JSA

• Entry DOI: 10.2210/pdb2jsa/pdb
• Related: 2JS9
• NMR Information: BMRB: 15358
• Descriptor: Saposin-like protein family protein 5 (1 entity in total)
• Functional Keywords: caenopore-5, saposin-like fold, antimicrobial protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 1
• Total formula weight: 11010.46

Authors

Mysliwy, J.,Grotzinger, J. (deposition date: 2007-07-02, release date: 2008-10-14, Last modification date: 2024-10-16)

Primary citation

Mysliwy, J.,Dingley, A.J.,Stanisak, M.,Jung, S.,Lorenzen, I.,Roeder, T.,Leippe, M.,Grotzinger, J.
Caenopore-5: the three-dimensional structure of an antimicrobial protein from Caenorhabditis elegans.
Dev.Comp.Immunol., 34:323-330, 2010

PubMed Abstract: 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.

PubMed: 19917307
DOI: 10.1016/j.dci.2009.11.003

Experimental method

SOLUTION NMR