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3.4.24.69: bontoxilysin

This is an abbreviated version!
For detailed information about bontoxilysin, go to the full flat file.

Word Map on EC 3.4.24.69

Reaction

Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or syntaxin. No detected action on small molecule substrates =

Synonyms

abobotulinumtoxinA, antigen E, Balc424, BoNT, BoNT A, BoNT B, BoNT E, BoNT F, BoNT F/A, BoNT LC, BoNT LC/A, BoNT serotype A, BoNT serotype E, BoNT serotype F, BoNT-A, BoNT-C, BoNT-D, BoNT-E, BoNT-F, BoNT/A, BoNT/A LC, BoNT/A Lc endopeptidase, BoNT/A-LC, BoNT/A1, BoNT/A2, BoNT/A3, BoNT/A4, BoNT/A5, BoNT/A6, BoNT/A8, BoNT/B, BoNT/B light chain protease, BoNT/B-LC, BoNT/B1, BoNT/B6, BoNT/C, BoNT/C1, BoNT/C1-LC, BoNT/C3, BoNT/CD, BoNT/D, BoNT/E, BoNT/F, BoNT/F proteolytic F toxin, BoNT/F-LC, BoNT/F1, BoNT/F5, BoNT/F6, BoNT/F7, BoNT/F9, BoNT/FA, BoNT/G, BoNT/HA, BoNT/T, BoNT/X, BoNTA, BoNTA endopeptidase, BoNTB, BoNTC, BoNTE, BoNTF, Bontoxilysin C1, botox A, botulinum A neurotoxin light chain, Botulinum neurotoxin, botulinum neurotoxin a, botulinum neurotoxin A light chain, botulinum neurotoxin A protease, botulinum neurotoxin A subtype 1, botulinum neurotoxin A subtype 2, botulinum neurotoxin A subtype 6, botulinum neurotoxin A3, botulinum neurotoxin A4, botulinum neurotoxin A8 subtype, botulinum neurotoxin B, botulinum neurotoxin B protease, botulinum neurotoxin C, botulinum neurotoxin D light chain, botulinum neurotoxin E, botulinum neurotoxin endopeptidase, botulinum neurotoxin F, botulinum neurotoxin serotype A, botulinum neurotoxin serotype A endopeptidase, botulinum neurotoxin serotype A light chain, botulinum neurotoxin serotype A protease, botulinum neurotoxin serotype B, botulinum neurotoxin serotype BA, botulinum neurotoxin serotype C1, botulinum neurotoxin serotype C1 light chain protease, botulinum neurotoxin serotype D, botulinum neurotoxin serotype E, botulinum neurotoxin serotype F, botulinum neurotoxin serotype FA, botulinum neurotoxin serotype G, botulinum neurotoxin serotype H, botulinum neurotoxin subtype A, botulinum neurotoxin subtype A3, botulinum neurotoxin subtype A4, botulinum neurotoxin subtype B6, botulinum neurotoxin subtype F5, botulinum neurotoxin type A, botulinum neurotoxin type A light chain, botulinum neurotoxin type B, botulinum neurotoxin type C, botulinum neurotoxin type D, botulinum neurotoxin type E, botulinum neurotoxin type F, botulinum neurotoxin type F light chain, botulinum neurotoxin type G, botulinum neurotoxin type HA, botulinum neurotoxin X, Botulinum neurotoxin-A, botulinum toxin, botulinum toxin C3, botulinum toxin serotype E, botulinum toxin serotype F, botulinum toxin type A, botulinum toxin type B, botulinum toxin type F, Botulinumtoxin A, BoTxA, C2 toxin, CDC69016, Clostridium botulinum A2 neurotoxin, Clostridium botulinum C2 toxin, Clostridium botulinum neurotoxin, Clostridium botulinum neurotoxin A1, Clostridium botulinum neurotoxin F, Clostridium botulinum neurotoxin serotype A, Clostridium botulinum neurotoxin serotype A light chain, Clostridium botulinum neurotoxin type E, Clostridium botulinum serotype D neurotoxin, CNT endopeptidase, D-4947 L-TC, daxibotulinumtoxinA, HCB, HCE, incobotulinumtoxinA, LC/A, LC/D, LC/F5, LC/HA, LC/X, LCA, LcB, lcc1, LCD, LCE, LCF, LHn/D, More, mosaic toxin, neurotoxin A, NT, onabotulinumtoxinA, serotype D botulinum neurotoxin, subtype A4 neurotoxin, TeNT, Tetanus neurotoxin, type A BoNT, type A botulinum neurotoxin, type A botulinum neurotoxin light chain, type A botulinum neurotoxin protease, type F toxin

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.69 bontoxilysin

Crystallization

Crystallization on EC 3.4.24.69 - bontoxilysin

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
binding domain of subtype BoNT/, sitting drop vapor diffusion method, using 10 mM spermine tetrahydrochloride, 10 mM spermidine trihydrochloride, 10 mM 1,4-diaminobutane dihydrochloride, 10 mM DL-ornithine monohydrochloride, 0.1 M MOPSO/bis-Tris pH 6.5, 15% (w/v) PEG 3 K, 20% (w/v), 1,2,4-butanetriol, 1% (w/v) NDSB 256
binding domain of subtype BoNT/A4, sitting drop vapor diffusion method, using 10 mM spermine tetrahydrochloride, 10 mM spermidine trihydrochloride, 10 mM 1,4-diaminobutane dihydrochloride, 10 mM DL-ornithine monohydrochloride, 0.1 M MOPSO/bis-Tris pH 6.5, 15% (w/v) PEG 3 K, 20% (w/v), 1,2,4-butanetriol, 1% (w/v) NDSB 256
BoNT E holotoxin, sitting-drop vapor diffusion, 8 mg/ml toxin in 50 mM HEPES buffer and 100 mM NaCl at pH 7.0, is mixed in a 1:1 ratio with reservoir solution containing 10% PEG 8000, 100 mM NaCl, and 100 mM HEPES at pH 7.0 at 18 °C, crystals appear after 1 weeks and grow to full-size within 2 weeks, X-ray diffraction structure determination and analysis at 2.65 A resolution
BoNT/F in complex with inhibitors VAMP 22-58/Gln58D-cysteine and VAMP 27-58/Gln58D-cysteine, X-ray diffraction structure determination and analysis at 2.1 A and 2.17 A resolution, respectively
botulinum neurotoxin A-receptor-binding domain in complex with the SV2C luminal domain, vapor diffusion method, using 100 mM HEPES, pH 7.5, 6% (w/v) PEG 8000, 8% (v/v) glycerol and 100 mM NaCl
P10845
botulinum neurotoxin E light chain, sitting drop vapor diffusion method
-
catalytic and translocation domain of botulinum neurotoxin type D, sitting drop vapor diffusion method, using 0.1 M sodium actetate pH 5.5, 0.8 M sodium formate, 10% (w/v) polyethylene glycol 8000, 10% (w/v) polyethylene glycol 1000
complex between the botulinum neurotoxin A light chain and the inhibitory peptide N-Ac-CRATKML, X-ray diffraction structure determination and analysis at 1.4 A resolution, and in a second approach unliganded enzyme light chain with and without the Zn2+ cofactor bound, X-ray diffraction structure determination and anaylsis at 1.25 A and 1.20 A resolution, respectively, 6-8 mg/ml purified BoNT/ALC, residues 1-425, in 50 mM NaPO4, pH 6.0, and 2 mM EDTA, hanging drop vapor diffusion method, mixing of protein solution with reservoir solution containing 20% PEG 3,350, 0.2 M diammonium tartrate, pH 6.6, and equilibration against 0.5 ml reservoir solution, the crystals are soaked prior to cryo-cooling in the crystallization solution plus 10 mM Zn(NO3)2 for 4.5 h or 5 mM Zn(NO3)2 and 2 mM N-Ac-CRATKML for 23 h, respectively, modeling
P10845
complex of botulinum neurotoxin serotype A protease bound to human SNAP-25, 2.1 A resolution
-
crystal structure of BoNT/CD-HCR (S867-E1280) is determined at 1.56 A resolution and compared to previously reported structures for BoNT/DHCR. The BoNT/CD-HCR structure is similar to the two sub-domain organization observed for other BoNT HCRs: an N-terminal jellyroll barrel motif and a C-terminal beta-trefoil fold
enzyme in a product-bound state, hanging drop vapor diffusion
-
full length Clostridium botulinum neurotoxin type E light chain, sitting drop vapor diffusion method, crystals diffract to better than 2.1 A, crystals belong to space group P2(1)2(1)2 with cell dimensions a = 88.33 A, b = 144.45 A, c = 83.37 A
-
hanging drop vapor diffusion at 22°C, crystal structure of Clostridium botulinum neurotoxin protease in a product-bound state
-
hanging drop vapor diffusion method, using either 19% (w/v) PEG1500, 0.1 M MMT pH 6.0 or 11% (w/v) PEG20000, 0.1 M MES pH 6.5, 10 mM EDTA
hemagglutinin 33 component of botulinum neurotoxin type B progenitor toxin complex bound to lactose, hanging drop vapor diffusion method, using 0.1 M HEPES (pH 7.0), 5% MPD, 5% (w/v) PEG [poly(ethylene glycol)] 6k, and 20 mM lactose
-
high-resolution structure of botulinum neurotoxin serotype F light chain in two crystal forms, sitting drop vapor diffusion method
-
in complex with non-toxic non-hemagglutinin protein, small-angle X-ray scattering
P10845
light chain protease domain of botulinum neurotoxin type HA, hanging drop vapor diffusion method, using 100 mM calcium acetate, 100 mM sodium cacodylate, pH 5.5 and 4% (w/v) polyethylene glycol 8000
-
mutant enzyme E1191M/S1199Y in complex with synaptotagmin 1, sitting drop vapor diffusion method, using 1.1 M sodium malonate dibasic monohydrate, HEPES (pH 7.0), and 0.5% (v/v) Jeffamine ED-2003. Mutant enzyme E1191M/S1199Y in complex with synaptotagmin 2, sitting drop vapor diffusion method, using 0.2 M MgCl2, Tris (pH 7.0), and 10% (w/v) PEG 8000
-
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
-
nanodroplet vapor diffusion method, crystal structure of botulinum neurotoxin type G light chain at 2.35 A resolution
-
purified recombinant enzyme free or in complex with substrate analogue inhibitor peptides, sitting drop vapor diffusion method at room temperature, 0.002 ml of 20 mg/ml enzyme in 2 mM DTT, 200 mM NaCl, and 20 mM HEPES, pH 7.4, is mixed with 0.002 ml reservoir solution containing 15% w/v PEG 3350, 0.3 M ammonium sulfate and 100 mM Bis-Tris buffer, pH 6.8 , equilibration against 0.8 ml of reservoir solution, plate-like crystals within a week, recombinant Balc424 is co-crystallized individually with the tetrapeptides, sitting drop vapor diffusion method at room temperature using conditions similar to native protein, Balc424 gives good complex crystals with RRGC, RRGM, RRGL and RRGI at stoichiometric ratios of 1:30, 1:30, 1:40 and 1:40, respectively, X-ray diffraction structure determination and analysis at 1.6-1.8 A resolution
P10845
purified recombinant His-tagged BoNT/C1-LC, vapour diffusion method, 12 mg/ml protein in 20 mM HEPES, pH 7.4, is mixed with an equal volume of reservoir solution containing 1.6 M sodium formate and 0.1 M sodium citrate, pH 4.6-5.0, 4°C, cryoprotection in the same mother liquor supplemented with 20% glycerol, X-ray structure determination and analysis at 1.75 A resolution, molecular replacement
-
purified recombinant His-tagged BoNT/G HCR, hanging drop vapour diffusion method, 11.5 mg/mL protein in mother liquor containing 12-15% w/v PEG 3350, 20 mM Bis-Tris buffer, pH 5.75-6.5, and 20-25 mM MgCl, X-ray diffraction structure determination and analysis at 2.0 A resolution, modelling
purified recombinant His-tagged truncated enzyme, residues 1-424, in complex with inhibitors 4-chlorocinnamic hydroxamate, 2,4-dichlorocinnamic hydroxamate, and L-arginine hydroxamate, hanging drop vapor diffusion method, drops are formed of equal parts BoNT/A-LC(1-424) at 10 mg/ml in 20 mM HEPES, pH 7.5, 50 mM NaCl and well solution containing 10%-15% PEG-2000 monomethyl ether, 0.3M(NH4)2HPO4, 50 mM Tris, pH 8.5, co-crystallization with inhibitor by addition of 0.5 mM ligand to the protein solution, 1.3 days, larger crystals by microseeding, X-ray diffraction structure determination and analysis at 1.9-2.5 A resolution, modeling
-
purified recombinant native and SeMet-derivative enzyme, mixing of 0.001 ml protein solution containing 1 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 200 mM NaCl, with 0.001 ml reservoir buffer, containing 0.2 M potassium/sodium tartrate, 0.1 M trisodium citrate, pH 5.6, and 1 M ammonium sulfate for the native enzyme, and 0.1 M MES pH 6.5, 1.6 M magnesium sulfate, and 1 M sodium chloride for the selenium methionine-labeled enzyme, equilibration against 0.1 ml reservoir buffer, 20°C, X-ray diffraction structure determination and analysis at 2.8 A and 3.1 A resolution, respectively
purified recombinant protein consisting of the receptor-binding domain of botulinum neurotoxin serotype B fused to the luminal domain of synaptotagmin II, vapour diffusion method, 20°C, using first 13% PEG 6000 and 0.1 M HEPES pH 7.0, and second, 0.8 M sodium citrate, pH 6.5, X-ray diffraction structure detremination and analysis at 2.15 A resolution, molecular replacement and modeling
-
receptor binding domains of BoNT/A and BoNT/F
sructures of BoNT/A, BoNT/B, and BoNT/E holotoxins
-
subtype BoNT/B bound to both its protein receptor and ganglioside 1a, vapor diffusion method, using 0.2 M MgCl2, 0.1M HEPES pH 7.0-7.2 and 20-24% (w/v) PEG 6000
subtype BoNT/CD-heavy chain receptor binding domain, hanging drop vapor diffusion method, using 1.6 M (NH4)2SO4, 2% (w/v) PEG 400, and 0.1 M HEPES, pH 7.5
the crystal structure of the BoNT/F receptor-binding domain in complex with the sugar moiety of ganglioside GD1a is reported. GD1a binds in a shallow groove formed by a conserved peptide motif, with additional stabilizing interactions provided by two arginine residues