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1.C.8.1.3
Clostridium botulinum neurotoxin (BoNT) type E (The 3d structure is known (Kumaran et al., 2009)). BoNT consists of a light chain (L) and a heavy chain (H) linked by a disulfide bond, where the heavy chain is divided into a translocation domain and an acceptor binding domain (Hc). Tan et al. 2023 explored a recombinant L-HN fragment (EL-HN) composed of the L and HN domains of BoNT/E. Neurotoxicity of L-HN fragments was assessed in mice, and the receptor synaptic vesicle glycoprotein 2C (SV2C) was explored. The 50% mouse lethal dose of the nicked dichain EL-HN fragment (EL-HN-DC) was 0.5 mug, and its neurotoxicity was the highest among the L-HN's of the four serotypes of BoNT(A/B/E/F). The cleavage efficiency of EL-HN-DC toward synaptosome- associated protein 25 (SNAP25) in vitro was 3-fold higher than that of the single chain at the cellular level, and showed 200-fold higher animal toxicity. The EL-HN-DC fragment might enter  cells via binding to SV2C to efficiently cleave SNAP25. Thus, the EL-HN fragment showed good biological activity and could be used as a drug screening model and to further explore the molecular mechanism of its transmembrane transport (Tan et al. 2023).

Accession Number:Q00496
Protein Name:Botulinum neurotoxin type E
Length:1251
Molecular Weight:143844.00
Species:Clostridium botulinum [1491]
Location1 / Topology2 / Orientation3: Secreted1
Substrate peptide

Cross database links:

DIP: DIP-46083N
Pfam: PF01742    PF07951    PF07953    PF07952   

Gene Ontology

GO:0005829 C:cytosol
GO:0030666 C:endocytic vesicle membrane
GO:0044164 C:host cell cytosol
GO:0044156 C:host cell junction
GO:0044231 C:host cell presynaptic membrane
GO:0016021 C:integral to membrane
GO:0004222 F:metalloendopeptidase activity
GO:0050827 F:toxin receptor binding
GO:0008270 F:zinc ion binding
GO:0051609 P:inhibition of neurotransmitter uptake
GO:0009405 P:pathogenesis
GO:0006508 P:proteolysis

References (8)

[1] “Sequences of the botulinal neurotoxin E derived from Clostridium botulinum type E (strain Beluga) and Clostridium butyricum (strains ATCC 43181 and ATCC 43755).”  Poulet S.et.al.   1543481
[2] “The complete amino acid sequence of the Clostridium botulinum type-E neurotoxin, derived by nucleotide-sequence analysis of the encoding gene.”  Whelan S.M.et.al.   1541280
[3] “The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins.”  Binz T.et.al.   2160960
[4] “Partial amino acid sequences of botulinum neurotoxins types B and E.”  Schmidt J.J.et.al.   3888113
[5] “Botulinum neurotoxin type E fragmented with endoproteinase Lys-C reveals the site trypsin nicks and homology with tetanus neurotoxin.”  Gimenez J.A.et.al.   2116911
[6] “Gene probes for identification of the botulinal neurotoxin gene and specific identification of neurotoxin types B, E, and F.”  Campbell K.D.et.al.   8408542
[7] “Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds.”  Schiavo G.et.al.   8243676
[8] “Proteolysis of SNAP-25 by types E and A botulinal neurotoxins.”  Binz T.et.al.   8294407
Structure:
1T3A   1T3C   1ZKW   1ZKX   1ZL5   1ZL6   1ZN3   3FFZ     

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MPKINSFNYN DPVNDRTILY IKPGGCQEFY KSFNIMKNIW IIPERNVIGT TPQDFHPPTS 
61:	LKNGDSSYYD PNYLQSDEEK DRFLKIVTKI FNRINNNLSG GILLEELSKA NPYLGNDNTP 
121:	DNQFHIGDAS AVEIKFSNGS QDILLPNVII MGAEPDLFET NSSNISLRNN YMPSNHRFGS 
181:	IAIVTFSPEY SFRFNDNCMN EFIQDPALTL MHELIHSLHG LYGAKGITTK YTITQKQNPL 
241:	ITNIRGTNIE EFLTFGGTDL NIITSAQSND IYTNLLADYK KIASKLSKVQ VSNPLLNPYK 
301:	DVFEAKYGLD KDASGIYSVN INKFNDIFKK LYSFTEFDLR TKFQVKCRQT YIGQYKYFKL 
361:	SNLLNDSIYN ISEGYNINNL KVNFRGQNAN LNPRIITPIT GRGLVKKIIR FCKNIVSVKG 
421:	IRKSICIEIN NGELFFVASE NSYNDDNINT PKEIDDTVTS NNNYENDLDQ VILNFNSESA 
481:	PGLSDEKLNL TIQNDAYIPK YDSNGTSDIE QHDVNELNVF FYLDAQKVPE GENNVNLTSS 
541:	IDTALLEQPK IYTFFSSEFI NNVNKPVQAA LFVSWIQQVL VDFTTEANQK STVDKIADIS 
601:	IVVPYIGLAL NIGNEAQKGN FKDALELLGA GILLEFEPEL LIPTILVFTI KSFLGSSDNK 
661:	NKVIKAINNA LKERDEKWKE VYSFIVSNWM TKINTQFNKR KEQMYQALQN QVNAIKTIIE 
721:	SKYNSYTLEE KNELTNKYDI KQIENELNQK VSIAMNNIDR FLTESSISYL MKIINEVKIN 
781:	KLREYDENVK TYLLNYIIQH GSILGESQQE LNSMVTDTLN NSIPFKLSSY TDDKILISYF 
841:	NKFFKRIKSS SVLNMRYKND KYVDTSGYDS NININGDVYK YPTNKNQFGI YNDKLSEVNI 
901:	SQNDYIIYDN KYKNFSISFW VRIPNYDNKI VNVNNEYTII NCMRDNNSGW KVSLNHNEII 
961:	WTFEDNRGIN QKLAFNYGNA NGISDYINKW IFVTITNDRL GDSKLYINGN LIDQKSILNL 
1021:	GNIHVSDNIL FKIVNCSYTR YIGIRYFNIF DKELDETEIQ TLYSNEPNTN ILKDFWGNYL 
1081:	LYDKEYYLLN VLKPNNFIDR RKDSTLSINN IRSTILLANR LYSGIKVKIQ RVNNSSTNDN 
1141:	LVRKNDQVYI NFVASKTHLF PLYADTATTN KEKTIKISSS GNRFNQVVVM NSVGNCTMNF 
1201:	KNNNGNNIGL LGFKADTVVA STWYYTHMRD HTNSNGCFWN FISEEHGWQE K