Structural highlights
FunctionPublication Abstract from PubMedWe isolated oryctin, a 66-residue peptide, from the hemolymph of the coconut rhinoceros beetle Oryctes rhinoceros and cloned its cDNA. Oryctin is dissimilar to any other known peptides in amino acid sequence, and its function has been unknown. To reveal that function, we determined the solution structure of recombinant (13)C,(15)N-labeled oryctin by heteronuclear NMR spectroscopy. Oryctin exhibits a fold similar to that of Kazal-type serine protease inhibitors but has a unique additional C-terminal alpha-helix. We performed protease inhibition assays of oryctin against several bacterial and eukaryotic proteases. Oryctin does inhibit the following serine proteases: alpha-chymotrypsin, endopeptidase K, subtilisin Carlsberg, and leukocyte elastase, with K(i) values of 3.9 x 10(-10) m, 6.2 x 10(-10) m, 1.4 x 10(-9) m, and 1.2 x 10(-8) m, respectively. Although the target molecule of oryctin in the beetle hemolymph remains obscure, our results showed that oryctin is a novel single domain Kazal-type inhibitor and could play a key role in protecting against bacterial infections. Isolation, cDNA cloning, and structure-based functional characterization of oryctin, a hemolymph protein from the coconut rhinoceros beetle, Oryctes rhinoceros, as a novel serine protease inhibitor.,Horita S, Ishibashi J, Nagata K, Miyakawa T, Yamakawa M, Tanokura M J Biol Chem. 2010 Sep 24;285(39):30150-8. Epub 2010 Jul 14. PMID:20630859[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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