7WKF
Antimicrobial peptide-LaIT2
Summary for 7WKF
| Entry DOI | 10.2210/pdb7wkf/pdb |
| NMR Information | BMRB: 36469 |
| Descriptor | Beta-KTx-like peptide LaIT2 (1 entity in total) |
| Functional Keywords | cyana 2.1 scorpion antimicrobial peptide, structural protein |
| Biological source | Liocheles australasiae |
| Total number of polymer chains | 1 |
| Total formula weight | 6650.89 |
| Authors | Tamura, M.,Morita, H.,Ohki, S. (deposition date: 2022-01-09, release date: 2023-04-05, Last modification date: 2024-11-13) |
| Primary citation | Tamura, M.,Tatsushiro, C.,Morita, E.H.,Ohki, S. Structural and functional studies of LaIT2, an antimicrobial and insecticidal peptide from Liocheles australasiae. Toxicon, 214:8-17, 2022 Cited by PubMed Abstract: LaIT2, composed of 59 amino acid residues, is a peptide toxin isolated from the venom of the Yaeyama scorpion, Liocheles australasiae. LaIT2 is toxic to insects but not most mammals. The N- and C-domains of LaIT2 are known to possess antimicrobial and insecticidal activities, respectively. However, the molecular mechanisms are largely unknown because of the lack of a three-dimensional structure of LaIT2. Thus, we elucidated the solution NMR structure of LaIT2. LaIT2 adopts a β-KTx-like two-domain structure, in which the N- and C-terminal domains form a random coil and an α-β-β motif, respectively. Trifluoro ethanol and liposomes titration experiments showed that the unstructured N-domain of LaIT2 has the ability to form an α-helix. The N-terminal helix is amphiphilic, and one side of the helix is positively charged. Measurements of the antimicrobial and insecticidal activities of LaIT2 mutants suggested K15 in the N-domain was found to be responsible for the antimicrobial activities, whereas L53 and L54 in the C-domain were key residues involved in the insecticidal activity. Moreover, K21 in the N-domain is important for both activities. Therefore, two domains are suggested that they work together to show antimicrobial and insecticidal activity. PubMed: 35490851DOI: 10.1016/j.toxicon.2022.04.015 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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