| Autor: |
G. Marini, B. Poland, C. Leininger, N. Lukoyanova, D. Spielbauer, J. Barry, D. Altier, A. Lum, E. Scolaro, C. Pérez Ortega, N. Yalpani, G. Sandahl, T. Mabry, J. Klever, T. Nowatzki, J-Z. Zhao, A. Sethi, A. Kassa, V. Crane, A. Lu, M.E. Nelson, N. Eswar, M. Topf, H.R. Saibil |
| Rok vydání: |
2022 |
| Popis: |
Broad adoption of transgenic crops has revolutionized agriculture. However, resistance to insecticidal proteins by agricultural pests poses a continuous challenge to maintaining crop productivity and new proteins are urgently needed to replace existing transgenic traits. We identified an insecticidal membrane attack complex/perforin (MACPF) protein, Mpf2Ba1, with strong activity against western corn rootworm larvae and a novel site of action. By integrating X-ray crystallography, cryo-EM, and modelling, we determined monomeric, pre-pore and pore structures, revealing changes between structural states at atomic resolution. We discovered a monomer inhibition mechanism, a molecular “switch” associated with pre-pore activation/oligomerization upon gut fluid incubation and solved the highest resolution MACPF pore structure to-date. Our findings provide a mechanistic basis for Mpf2Ba1 effectiveness as an insecticidal protein with potential for biotechnology development.One-Sentence SummaryThe molecular mechanism of an insecticidal protein is revealed through 3D structures of the three main pore formation states |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
