2RQ2
The solution structure of the N-terminal fragment of big defensin
Summary for 2RQ2
| Entry DOI | 10.2210/pdb2rq2/pdb |
| NMR Information | BMRB: 11072 |
| Descriptor | Big defensin (1 entity in total) |
| Functional Keywords | antimicrobial peptide, antibiotic, antimicrobial, fungicide, secreted |
| Total number of polymer chains | 1 |
| Total formula weight | 2887.33 |
| Authors | Kouno, T.,Mizuguchi, M.,Aizawa, T.,Shinoda, H.,Demura, M.,Kawabata, S.,Kawano, K. (deposition date: 2009-01-07, release date: 2009-08-25, Last modification date: 2024-05-15) |
| Primary citation | Kouno, T.,Mizuguchi, M.,Aizawa, T.,Shinoda, H.,Demura, M.,Kawabata, S.,Kawano, K. A novel beta-defensin structure: big defensin changes its N-terminal structure to associate with the target membrane Biochemistry, 48:7629-7635, 2009 Cited by PubMed Abstract: Big defensin is a 79-residue peptide derived from hemocytes of the Japanese horseshoe crab. The amino acid sequence of big defensin is divided into an N-terminal hydrophobic domain and a C-terminal cationic domain, which are responsible for antimicrobial activities against Gram-positive and -negative bacteria, respectively. The N-terminal domain of big defensin forms a unique globular conformation with two alpha-helices and a parallel beta-sheet, while the C-terminal domain adopts a beta-defensin-like fold. Although our previous study implied that big defensin changes its N-terminal structure in a micellar environment, due to the poor quality of the NMR spectra it remained to be resolved whether the N-terminal domain adopts any structure in the presence of micelles. In this analysis, we successfully determined the structure of the N-terminal fragment of big defensin in a micellar solution, showing that the fragment peptide forms a single alpha-helix structure. Moreover, NMR experiments using paramagnetic probes revealed that the N-terminal domain of big defensin penetrates into the micelle with a dipping at the N-terminal edge of the alpha-helix. Here, we propose a model for how big defensin associates with the target membrane. PubMed: 19588912DOI: 10.1021/bi900756y PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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