2js9
From Proteopedia
Structure of caenopore-5 (81 Pro cis conformer)
Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Caenopore-5: the three-dimensional structure of an antimicrobial protein from Caenorhabditis elegans.,Mysliwy J, Dingley AJ, Stanisak M, Jung S, Lorenzen I, Roeder T, Leippe M, Grotzinger J Dev Comp Immunol. 2010 Mar;34(3):323-30. Epub 2009 Nov 26. PMID:19917307[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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