6HOX
Crystal structure of the binding domain of Paraclostridial Mosquitocidal Protein 1
Summary for 6HOX
| Entry DOI | 10.2210/pdb6hox/pdb |
| Descriptor | Binding domain (Hc) of Paraclostridial Mosquitocidal Protein 1, DI(HYDROXYETHYL)ETHER, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | neurotoxin, botulinum, paraclostridium bifermentans, anopheles, toxin |
| Biological source | Paraclostridium bifermentans |
| Total number of polymer chains | 1 |
| Total formula weight | 52910.54 |
| Authors | Masuyer, G.,Stenmark, P. (deposition date: 2018-09-18, release date: 2019-07-10, Last modification date: 2024-01-24) |
| Primary citation | Contreras, E.,Masuyer, G.,Qureshi, N.,Chawla, S.,Dhillon, H.S.,Lee, H.L.,Chen, J.,Stenmark, P.,Gill, S.S. A neurotoxin that specifically targets Anopheles mosquitoes. Nat Commun, 10:2869-2869, 2019 Cited by PubMed Abstract: Clostridial neurotoxins, including tetanus and botulinum neurotoxins, generally target vertebrates. We show here that this family of toxins has a much broader host spectrum, by identifying PMP1, a clostridial-like neurotoxin that selectively targets anopheline mosquitoes. Isolation of PMP1 from Paraclostridium bifermentans strains collected in anopheline endemic areas on two continents indicates it is widely distributed. The toxin likely evolved from an ancestral form that targets the nervous system of similar organisms, using a common mechanism that disrupts SNARE-mediated exocytosis. It cleaves the mosquito syntaxin and employs a unique receptor recognition strategy. Our research has an important impact on the study of the evolution of clostridial neurotoxins and provides the basis for the use of P. bifermentans strains and PMP1 as innovative, environmentally friendly approaches to reduce malaria through anopheline control. PubMed: 31253776DOI: 10.1038/s41467-019-10732-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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