1zb7
From Proteopedia
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Crystal Structure of Botulinum Neurotoxin Type G Light Chain
Overview
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.
About this Structure
1ZB7 is a Single protein structure of sequence from Clostridium botulinum with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of botulinum neurotoxin type G light chain: serotype divergence in substrate recognition., Arndt JW, Yu W, Bi F, Stevens RC, Biochemistry. 2005 Jul 19;44(28):9574-80. PMID:16008342
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