3N7M

Crystal structure of W1252A mutant of HCR D/C VPI 5995

Summary for 3N7M

• Entry DOI: 10.2210/pdb3n7m/pdb
• Related: 3N7J 3N7K 3N7L
• Descriptor: Neurotoxin, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: botulinum neurotoxin, w1252a mutant, gm1a, ganglioside binding loop, toxin
• Biological source: Clostridium botulinum
• Total number of polymer chains: 1
• Total formula weight: 49111.20

Authors

Fu, Z.,Karalewitz, A.,Kroken, A.,Baldwin, M.R.,Barbieri, J.T.,Kim, J.-J.P. (deposition date: 2010-05-27, release date: 2010-09-08, Last modification date: 2023-09-06)

Primary citation

Karalewitz, A.P.,Kroken, A.R.,Fu, Z.,Baldwin, M.R.,Kim, J.J.,Barbieri, J.T.
Identification of a Unique Ganglioside Binding Loop within Botulinum Neurotoxins C and D-SA .
Biochemistry, 49:8117-8126, 2010

PubMed Abstract: The botulinum neurotoxins (BoNTs) are the most potent protein toxins for humans. There are seven serotypes of BoNTs (A-G) based on a lack of cross antiserum neutralization. BoNTs utilize gangliosides as components of the host receptors for binding and entry into neurons. Members of BoNT/C and BoNT/D serotypes include mosaic toxins that are organized in D/C and C/D toxins. One D/C mosaic toxin, BoNT/D-South Africa (BoNT/D-SA), was not fully neutralized by immunization with BoNT serotype C or D, which stimulated this study. Here the crystal structures of the receptor binding domains of BoNT/C, BoNT/D, and BoNT/D-SA are presented. Biochemical and cell binding studies show that BoNT/C and BoNT/D-SA possess unique mechanisms for ganglioside binding. These studies provide new information about how the BoNTs can enter host cells as well as a basis for understanding the immunological diversity of these neurotoxins.

PubMed: 20731382
DOI: 10.1021/bi100865f

Experimental method

X-RAY DIFFRACTION (2.6 Å)