2RNG
Solution structure of big defensin
Summary for 2RNG
| Entry DOI | 10.2210/pdb2rng/pdb |
| NMR Information | BMRB: 11022 |
| Descriptor | Big defensin (1 entity in total) |
| Functional Keywords | alpha-helices & beta-sheets, three disulfide bridges, antibiotic, antimicrobial, fungicide, secreted, antimicrobial protein |
| Biological source | Tachypleus tridentatus (Japanese horseshoe crab) |
| Total number of polymer chains | 1 |
| Total formula weight | 8646.87 |
| Authors | Kouno, T.,Fujitani, N.,Osaki, T.,Kawabata, S.,Nishimura, S.,Mizuguchi, M.,Aizawa, T.,Demura, M.,Nitta, K.,Kawano, K. (deposition date: 2007-12-27, release date: 2008-10-14, Last modification date: 2024-10-30) |
| Primary citation | Kouno, T.,Fujitani, N.,Mizuguchi, M.,Osaki, T.,Nishimura, S.,Kawabata, S.,Aizawa, T.,Demura, M.,Nitta, K.,Kawano, K. A novel beta-defensin structure: a potential strategy of big defensin for overcoming resistance by Gram-positive bacteria Biochemistry, 47:10611-10619, 2008 Cited by PubMed Abstract: Big defensin is a 79-residue peptide derived from hemocytes of the Japanese horseshoe crab. It has antimicrobial activities against Gram-positive and -negative bacteria. The amino acid sequence of big defensin can be divided into an N-terminal hydrophobic half and a C-terminal cationic half. Interestingly, the trypsin cleaves big defensin into two fragments, the N-terminal and C-terminal fragments, which are responsible for antimicrobial activity against Gram-positive and -negative bacteria, respectively. To explore the antimicrobial mechanism of big defensin, we determined the solution structure of mature big defensin and performed a titration experiment with DPC micelles. Big defensin has a novel defensin structure; the C-terminal domain adopts a beta-defensin structure, and the N-terminal domain forms a unique globular conformation. It is noteworthy that the hydrophobic N-terminal domain undergoes a conformational change in micelle solution, while the C-terminal domain remains unchanged. Here, we propose that the N-terminal domain achieves its antimicrobial activity in a novel fashion and explain that big defensin has developed a strategy different from those of other beta-defensins to suppress the growth of Gram-positive bacteria. PubMed: 18785751DOI: 10.1021/bi800957n PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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