| General information | | DisProt: | DP00732_C001 | | Name: | Botulinum neurotoxin type E light chain | | Synonym(s): | BXE_CLOBO
Bontoxilysin-E LC
Cleavage product 1 of Botulinum neurotoxin type E (aa 2-422)
BoNT/E-LC
| | First appeared in release: | Release 6.01 (10/15/2012) | | UniProt: | Q00496 | | UniGene: | | | SwissProt: | BXE_CLOBO | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Clostridium botulinum | | Sequence length: | 421 | | Percent disordered: | 5% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
PKINSFNYND PVNDRTILYI KPGGCQEFYK SFNIMKNIWI IPERNVIGTT PQDFHPPTSL - 60
KNGDSSYYDP NYLQSDEEKD RFLKIVTKIF NRINNNLSGG ILLEELSKAN PYLGNDNTPD - 120
NQFHIGDASA VEIKFSNGSQ DILLPNVIIM GAEPDLFETN SSNISLRNNY MPSNHRFGSI - 180
AIVTFSPEYS FRFNDNCMNE FIQDPALTLM HELIHSLHGL YGAKGITTKY TITQKQNPLI - 240
TNIRGTNIEE FLTFGGTDLN IITSAQSNDI YTNLLADYKK IASKLSKVQV SNPLLNPYKD - 300
VFEAKYGLDK DASGIYSVNI NKFNDIFKKL YSFTEFDLRT KFQVKCRQTY IGQYKYFKLS - 360
NLLNDSIYNI SEGYNINNLK VNFRGQNANL NPRIITPITG RGLVKKIIRF CKNIVSVKGI - 420
R
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| Functional narrative |
DP00732_C001 is cleavage product 1 of Botulinum neurotoxin type E, comprising aa P2-R422 of the parent protein.
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Function: Botulinum toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the 180-Arg-|-Ile- 181 bond in SNAP-25.
CATALYTIC ACTIVITY: Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
SUBUNIT: Disulfide-linked heterodimer of a light chain (L) and a heavy chain (H). The light chain has the pharmacological activity, while the N- and C-terminal of the heavy chain mediate channel formation and toxin binding, respectively.
Subcellular Location: Botulinum neurotoxin E light chain: Secreted. Host cytoplasm, host cytosol.
Subcellular Location: Botulinum neurotoxin E heavy chain: Secreted. Host cell junction, host synapse, host presynaptic cell membrane (Potential).
MISCELLANEOUS: There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C1, D, E, F, and G.
SIMILARITY: Belongs to the peptidase M27 family.
WEB RESOURCE: Name=BotDB - A Database Resource for Clostridial Neurotoxins; URL='http://botdb.abcc.ncifcrf.gov/';
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|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered | | Name: | disordered loop | | Location: | 234 - 244 | | Length: | 11 | | Region sequence: |
QKQNPLITNIR | | Modification type: | Native
| | PDB: | 1T3A:A, 1T3C:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (298 K; pH: 5.6; Ammonium sulfate 0.5 M; BoNT/E-LC (WT for PDB 1T3A, E212Q mut for PDB 1T3C); Lithium sulfate 1 M; Sodium citrate 0.1 M; Zn2+)
| References:
- Agarwal R, Eswaramoorthy S, Kumaran D, Binz T, Swaminathan S. "Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212-->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway." Biochemistry. 2004; 43(21): 6637-44. PubMed: 15157097
| Comments:According to Agarwal et al (2004), the disordered loop at Q234-R244 (PDB 1T3A) becomes ordered in the E212Q mutant (PDB 1T3C), "confirming that the missing residues are not due to any proteolysis."
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| Region 2 | | Type: | Disordered | | Name: | C-terminal | | Location: | 412 - 421 | | Length: | 10 | | Region sequence: |
KNIVSVKGIR | | Modification type: | Native
| | PDB: | 1T3A:A, 1T3C:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (298 K; pH: 5.6; Ammonium sulfate 0.5 M; BoNT/E-LC (WT for PDB 1T3A, E212Q mut for PDB 1T3C); Lithium sulfate 1 M; Sodium citrate 0.1 M; Zn2+)
| References:
- Agarwal R, Eswaramoorthy S, Kumaran D, Binz T, Swaminathan S. "Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212-->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway." Biochemistry. 2004; 43(21): 6637-44. PubMed: 15157097
| Comments:
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| Comments |
AV sent 10/1/2012 (PMID 15157097)
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