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Literature summary for 3.4.24.69 extracted from

  • Arndt, J.W.; Chai, Q.; Christian, T.; Stevens, R.C.
    Structure of botulinum neurotoxin type D light chain at 1.65 A resolution: repercussions for VAMP-2 substrate specificity (2006), Biochemistry, 45, 3255-3262.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
nanodroplet vapor diffusion method, 1.65 A resolution crystal structure of the catalytic domain of BoNT serotype D light chain. Structural analysis has identified a hydrophobic pocket potentially involved in substrate recognition of the P1' VAMP residue (Leu 60) and a second remote site for recognition of the V1 SNARE motif that is critical for activity. A structural comparison of BoNT/D-LC with BoNT/F-LC that also recognizes VAMP-2 one residue away from the BoNT/D-LC site provides additional molecular details about the unique serotype specific activities. In particular, BoNT/D prefers a hydrophobic interaction for the V1 motif of VAMP-2, while BoNT/F adopts a more hydrophilic strategy for recognition of the same V1 motif Clostridium botulinum

Organism

Organism UniProt Comment Textmining
Clostridium botulinum
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-
-

Purification (Commentary)

Purification (Comment) Organism
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Clostridium botulinum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
vesicle-associated membrane protein VAMP-2 + H2O
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Clostridium botulinum ?
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?

Synonyms

Synonyms Comment Organism
BoNT/D
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Clostridium botulinum
botulinum neurotoxin type D
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Clostridium botulinum