Journal
BIOCHEMISTRY
Volume 44, Issue 28, Pages 9574-9580Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi0505924
Keywords
-
Categories
Funding
- NCI NIH HHS [Y1-CO-1020] Funding Source: Medline
- NIAID NIH HHS [U54 AI065359-040013, U54 AI065359] Funding Source: Medline
- NIEHS NIH HHS [27301C0040] Funding Source: Medline
- NIGMS NIH HHS [Y1-GM-1104] Funding Source: Medline
Ask authors/readers for more resources
The seven serotypes (A-G) of botulinum neurotoxins (BoNTs) block neurotransmitter release through their specific proteolysis of one of the three proteins of the soluble N-ethylmaleimide-sensitive-factor attachment protein receptor (SNARE) complex. BoNTs have stringent substrate specificities that are unique for metalloprotease in that they require exceptionally long substrates (1). To understand the molecular reasons for the unique specificities of the BoNTs, we determined the crystal structure of the catalytic light chain (LC) of Clostridium botulinum neurotoxin type G (BoNT/G-LC) at 2.35 angstrom resolution. The structure of BoNT/G-LC reveals a C-terminal beta-sheet that is critical for LC oligomerization and is unlike that seen in the other LC structures. Its structural comparison with thermolysin and the available pool of LC structures reveals important serotype differences that are likely to be involved in substrate recognition of the P1' residue. In addition, structural and sequence analyses have identified a potential exosite of BoNT/G-LC that recognizes a SNARE recognition motif of VAMP.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available