PDBsum entry 4zkt

Hydrolase/toxin

PDB id: 4zkt

Contents

Protein chains

1235 a.a.

1114 a.a.

Metals

_ZN ×3

PDB id:

4zkt

Name:

Hydrolase/toxin

Title:

Crystal structure of the progenitor m complex of clostridium botulinum type e neurotoxin

Structure:

Bontoxilysin a. Chain: a, c, e. Botulinum neurotoxin type e, nontoxic-nonhemagglutinin component, ntnh. Chain: b, d, f

Source:

Clostridium botulinum (strain alaska e43 / type e3). Organism_taxid: 508767. Strain: alaska e43 / type e3. Strain: alaska e43 / type e3

Resolution:

3.05Å R-factor: 0.244 R-free: 0.321

Authors:

S.Eswaramoorthy,S.Swaminathan

Key ref:

S.Eswaramoorthy et al. (2015). Molecular Assembly of Clostridium botulinum progenitor M complex of type E. Sci Rep, 5, 17795. PubMed id: 26639353 DOI: 10.1038/srep17795

Date:

30-Apr-15 Release date: 23-Dec-15

Protein chains

A0A0X1KH89  (A0A0X1KH89_CLOBA) -  Bontoxilysin A from Clostridium botulinum (strain Alaska E43 / Type E3)

Seq: 1252 a.a.

Struc: 1235 a.a.

Protein chains

A0A0X1KH90  (A0A0X1KH90_CLOBA) -  Botulinum neurotoxin type E, nontoxic-nonhemagglutinin component, NTNH from Clostridium botulinum (strain Alaska E43 / Type E3)

Seq: 1163 a.a.

Struc: 1114 a.a.

Enzyme reactions

• Enzyme class: Chains A, C, E: E.C.3.4.24.69 - bontoxilysin.
• Reaction: Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.
• Cofactor: Zn(2+)

DOI no: 10.1038/srep17795

Sci Rep 5:17795 (2015)

PubMed id: 26639353

Molecular Assembly of Clostridium botulinum progenitor M complex of type E.

S.Eswaramoorthy, J.Sun, H.Li, B.R.Singh, S.Swaminathan.

ABSTRACT

Clostridium botulinum neurotoxin (BoNT) is released as a progenitor complex, in association with a non-toxic-non-hemagglutinin protein (NTNH) and other associated proteins. We have determined the crystal structure of M type Progenitor complex of botulinum neurotoxin E [PTC-E(M)], a heterodimer of BoNT and NTNH. The crystal structure reveals that the complex exists as a tight, interlocked heterodimer of BoNT and NTNH. The crystal structure explains the mechanism of molecular assembly of the complex and reveals several acidic clusters at the interface responsible for association at low acidic pH and disassociation at basic/neutral pH. The similarity of the general architecture between the PTC-E(M) and the previously determined PTC-A(M) strongly suggests that the progenitor M complexes of all botulinum serotypes may have similar molecular arrangement, although the neurotoxins apparently can take very different conformation when they are released from the M complex.