Literature summary for 3.4.24.69 extracted from

Kumaran, D.; Eswaramoorthy, S.; Furey, W.; Navaza, J.; Sax, M.; Swaminathan, S.
Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation (2009), J. Mol. Biol., 386, 233-245.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Clostridium botulinum

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the active-site zinc is coordinated by His212, His216, and Glu251, and nucleophilic water, which in turn is hydrogen-bonded to Glu213. Tyr351 is close to both nucleophilic water and catalytic zinc	Clostridium botulinum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Clostridium botulinum	BoNT E first binds to GT1b on the presynaptic membrane, like all other BoNTs. In BoNT B, the sialic acid of the sialyllactose that partly mimics GT1b binds in a shallow cavity formed by Trp1261 and His1240,12 and interacts with Tyr1262 and His1240, binding mode, overviewThe GT1b binding site in BoNT E is similar to those in other BoNTs and tetanus neurotoxin	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Clostridium botulinum	Q00496	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	BoNT E first binds to GT1b on the presynaptic membrane, like all other BoNTs. In BoNT B, the sialic acid of the sialyllactose that partly mimics GT1b binds in a shallow cavity formed by Trp1261 and His1240,12 and interacts with Tyr1262 and His1240, binding mode, overviewThe GT1b binding site in BoNT E is similar to those in other BoNTs and tetanus neurotoxin	Clostridium botulinum	?	-	?
additional information	active site structure, Tyr351 is close to both nucleophilic water and catalytic zinc, overview	Clostridium botulinum	?	-	?

Subunits

Subunits	Comment	Organism
More	in BoNT E, both the binding domain and the catalytic domain are on the same side of the translocation domain, and all three have mutual interfaces. This unique association may have an effect on the rate of translocation, with the molecule strategically positioned in the vesicle for quick entry into cytosol. Separation of the domains causes conformational changes. Domain organization of BoNT E, modelling, overview	Clostridium botulinum

Synonyms

Synonyms	Comment	Organism
BoNT E	-	Clostridium botulinum
Clostridium botulinum neurotoxin type E	-	Clostridium botulinum

General Information

General Information	Comment	Organism
additional information	the translocation-competent conformation in BoNT E is a probable reason for its faster toxic rate compared to BoNT A	Clostridium botulinum
physiological function	botulism, the disease caused by BoNT E, sets in faster than any other serotype because of its speedy internalization and translocation, and the present structure offers a credible explanation	Clostridium botulinum

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Release 2023.1 (January 2023)