2KSW
Backbone 1H, 13C, and 15N Chemical Shift Assignments for Oryctin
2KSW の概要
| エントリーDOI | 10.2210/pdb2ksw/pdb |
| NMR情報 | BMRB: 16676 |
| 分子名称 | Oryctin (1 entity in total) |
| 機能のキーワード | kazal-type, protease inhibitor, hydrolase inhibitor |
| 由来する生物種 | Oryctes rhinoceros (Coconut rhinoceros beetle) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 7257.40 |
| 構造登録者 | Horita, S.,Ishibashi, J.,Nagata, K.,Miyakawa, T.,Yamakawa, M.,Tanokura, M. (登録日: 2010-01-14, 公開日: 2010-07-14, 最終更新日: 2024-11-13) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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