1ZB7

Crystal Structure of Botulinum Neurotoxin Type G Light Chain

Summary for 1ZB7

• Entry DOI: 10.2210/pdb1zb7/pdb
• Descriptor: neurotoxin, ZINC ION, CITRATE ANION, ... (4 entities in total)
• Functional Keywords: hexxh metalloprotease, toxin
• Biological source: Clostridium botulinum
• Cellular location: Secreted (By similarity): Q60393
• Total number of polymer chains: 1
• Total formula weight: 52197.31

Authors

Arndt, J.W.,Yu, W.,Bi, F.,Stevens, R.C. (deposition date: 2005-04-07, release date: 2005-07-05, Last modification date: 2024-10-30)

Primary citation

Arndt, J.W.,Yu, W.,Bi, F.,Stevens, R.C.
Crystal structure of botulinum neurotoxin type g light chain: serotype divergence in substrate recognition
Biochemistry, 44:9574-9580, 2005

PubMed Abstract: 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 A 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.

PubMed: 16008342
DOI: 10.1021/bi0505924

Experimental method

X-RAY DIFFRACTION (2.35 Å)