7PQW
NMR solution structure of BCR4
Summary for 7PQW
| Entry DOI | 10.2210/pdb7pqw/pdb |
| NMR Information | BMRB: 34667 |
| Descriptor | BCR4 (1 entity in total) |
| Functional Keywords | endosymbiosis pesticide antimicrobial disulfide rich peptide bcr1 family, antimicrobial protein |
| Biological source | Acyrthosiphon pisum (pea aphid) |
| Total number of polymer chains | 1 |
| Total formula weight | 5905.65 |
| Authors | Loth, K.,Paquet, F. (deposition date: 2021-09-20, release date: 2022-09-28, Last modification date: 2024-11-13) |
| Primary citation | Loth, K.,Parisot, N.,Paquet, F.,Terrasson, H.,Sivignon, C.,Rahioui, I.,Ribeiro Lopes, M.,Gaget, K.,Duport, G.,Delmas, A.F.,Aucagne, V.,Heddi, A.,Calevro, F.,da Silva, P. Aphid BCR4 Structure and Activity Uncover a New Defensin Peptide Superfamily. Int J Mol Sci, 23:-, 2022 Cited by PubMed Abstract: Aphids (Hemiptera: Aphidoidea) are among the most detrimental insects for agricultural plants, and their management is a great challenge in agronomical research. A new class of proteins, called Bacteriocyte-specific Cysteine-Rich (BCR) peptides, provides an alternative to chemical insecticides for pest control. BCRs were initially identified in the pea aphid . They are small disulfide bond-rich proteins expressed exclusively in aphid bacteriocytes, the insect cells that host intracellular symbiotic bacteria. Here, we show that one of the BCRs, BCR4, displays prominent insecticidal activity against the pea aphid, impairing insect survival and nymphal growth, providing evidence for its potential use as a new biopesticide. Our comparative genomics and phylogenetic analyses indicate that BCRs are restricted to the aphid lineage. The 3D structure of BCR4 reveals that this peptide belongs to an as-yet-unknown structural class of peptides and defines a new superfamily of defensins. PubMed: 36293341DOI: 10.3390/ijms232012480 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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