5MK8
Crystal structure of the receptor-binding domain of the FA hybrid Clostridium botulinum neurotoxin
Summary for 5MK8
| Entry DOI | 10.2210/pdb5mk8/pdb |
| Descriptor | Botulinum neurotoxin FA binding domain, FORMIC ACID, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | bacterial toxin toxin receptor binding domain jelly roll fold beta trefoil fold, toxin |
| Biological source | Clostridium botulinum |
| Total number of polymer chains | 2 |
| Total formula weight | 102557.15 |
| Authors | Davies, J.R.,Acharya, K.R. (deposition date: 2016-12-02, release date: 2018-03-28, Last modification date: 2024-10-23) |
| Primary citation | Davies, J.R.,Hackett, G.S.,Liu, S.M.,Acharya, K.R. High resolution crystal structures of the receptor-binding domain ofClostridium botulinumneurotoxin serotypes A and FA. PeerJ, 6:e4552-e4552, 2018 Cited by PubMed Abstract: The binding specificity of botulinum neurotoxins (BoNTs) is primarily a consequence of their ability to bind to multiple receptors at the same time. BoNTs consist of three distinct domains, a metalloprotease light chain (LC), a translocation domain (H) and a receptor-binding domain (H). Here we report the crystal structure of H/FA, complementing an existing structure through the modelling of a previously unresolved loop which is important for receptor-binding. Our H/FA structure also contains a previously unidentified disulphide bond, which we have also observed in one of two crystal forms of H/A1. This may have implications for receptor-binding and future recombinant toxin production. PubMed: 29576992DOI: 10.7717/peerj.4552 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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