2KSW
Backbone 1H, 13C, and 15N Chemical Shift Assignments for Oryctin
Summary for 2KSW
| Entry DOI | 10.2210/pdb2ksw/pdb |
| NMR Information | BMRB: 16676 |
| Descriptor | Oryctin (1 entity in total) |
| Functional Keywords | kazal-type, protease inhibitor, hydrolase inhibitor |
| Biological source | Oryctes rhinoceros (Coconut rhinoceros beetle) |
| Total number of polymer chains | 1 |
| Total formula weight | 7257.40 |
| Authors | Horita, S.,Ishibashi, J.,Nagata, K.,Miyakawa, T.,Yamakawa, M.,Tanokura, M. (deposition date: 2010-01-14, release date: 2010-07-14, Last modification date: 2024-11-13) |
| Primary citation | Horita, S.,Ishibashi, J.,Nagata, K.,Miyakawa, T.,Yamakawa, M.,Tanokura, M. 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 J.Biol.Chem., 285:30150-30158, 2010 Cited by PubMed Abstract: We 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 α-helix. We performed protease inhibition assays of oryctin against several bacterial and eukaryotic proteases. Oryctin does inhibit the following serine proteases: α-chymotrypsin, endopeptidase K, subtilisin Carlsberg, and leukocyte elastase, with K(i) values of 3.9 × 10(-10) m, 6.2 × 10(-10) m, 1.4 × 10(-9) m, and 1.2 × 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. PubMed: 20630859DOI: 10.1074/jbc.M110.124735 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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