5mk8

Crystal structure of the receptor-binding domain of the FA hybrid Clostridium botulinum neurotoxin

spinqualitylabelsall models 5mk8, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mk8 is a 2 chain structure with sequence from Clostridium botulinum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: CL, FMT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9R540_CLOBO Publication Abstract from PubMed 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 (HN) and a receptor-binding domain (HC). Here we report the crystal structure of HC/FA, complementing an existing structure through the modelling of a previously unresolved loop which is important for receptor-binding. Our HC/FA structure also contains a previously unidentified disulphide bond, which we have also observed in one of two crystal forms of HC/A1. This may have implications for receptor-binding and future recombinant toxin production. High resolution crystal structures of the receptor-binding domain of Clostridium botulinum neurotoxin serotypes A and FA.,Davies JR, Hackett GS, Liu SM, Acharya KR PeerJ. 2018 Mar 21;6:e4552. doi: 10.7717/peerj.4552. eCollection 2018. PMID:29576992 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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