PDBsum entry 1z0h

Hydrolase

PDB id

1z0h

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Contents

			Protein chains

					438 a.a. *

			Waters ×416

* Residue conservation analysis

PDB id:

1z0h

Links

Name:

Hydrolase

Title:

N-terminal helix reorients in recombinant c-fragment of clostridium botulinum type b

Structure:

Botulinum neurotoxin type b. Chain: a, b. Fragment: sequence database residues 853-1290. Synonym: bont/b, bontoxilysin b. Engineered: yes

Source:

Clostridium botulinum. Organism_taxid: 1491. Gene: botb. Expressed in: pichia pastoris. Expression_system_taxid: 4922

Resolution:

2.00Å

R-factor:

0.234

R-free:

0.282

Authors:

S.Jayaraman,S.Eswarmoorthy,S.A.Ashraf,L.A.Smith,S.Swaminathan

Key ref:

S.Jayaraman et al. (2005). N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B. Biochem Biophys Res Commun, 330, 97. PubMed id: 15781237 DOI: 10.1016/j.bbrc.2005.02.123

Date:

01-Mar-05

Release date:

15-Mar-05

PROCHECK

	Headers

	References

Protein chains

P10844 (BXB_CLOBO) - Botulinum neurotoxin type B from Clostridium botulinum

Seq: Struc:

Seq: Struc:

Seq: Struc:					1291 a.a. 438 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.3.4.24.69 - bontoxilysin.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

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: 10.1016/j.bbrc.2005.02.123	Biochem Biophys Res Commun 330:97 (2005)
PubMed id: 15781237

N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B.
S.Jayaraman, S.Eswaramoorthy, S.A.Ahmed, L.A.Smith, S.Swaminathan.

ABSTRACT

Botulinum neurotoxins comprise seven distinct serotypes (A-G) produced by Clostridium botulinum. The crystal structure of the binding domain of the botulinum neurotoxin type B (BBHc) has been determined to 2A resolution. The overall structure of BBHc is well ordered and similar to that of the binding domain of the holotoxin. However, significant structural changes occur at what would be the interface of translocation and binding domains of the holotoxin. The loop 911-924 shows a maximum displacement of 14.8A at the farthest point. The N-terminal helix reorients and moves by 19.5A from its original position. BBHc is compared with the binding domain of the holotoxin of botulinum type A and B, and the tetanus C-fragment to characterize the heavy chain-carbohydrate interactions. The probable reasons for different binding affinity of botulinum and tetanus toxins are discussed.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20233039

M.Montal (2010).
Botulinum neurotoxin: a marvel of protein design.

Annu Rev Biochem, 79, 591-617.

20877571

N.Gul, L.A.Smith, and S.A.Ahmed (2010).
Light chain separated from the rest of the type a botulinum neurotoxin molecule is the most catalytically active form.

PLoS One, 5, e12872.

20219474

P.Stenmark, M.Dong, J.Dupuy, E.R.Chapman, and R.C.Stevens (2010).
Crystal structure of the botulinum neurotoxin type G binding domain: insight into cell surface binding.

J Mol Biol, 397, 1287-1297.

PDB code:

2vxr

18704164

P.Stenmark, J.Dupuy, A.Imamura, M.Kiso, and R.C.Stevens (2008).
Crystal structure of botulinum neurotoxin type A in complex with the cell surface co-receptor GT1b-insight into the toxin-neuron interaction.

PLoS Pathog, 4, e1000129.

PDB codes:

2vu9 2vua

17167421

R.Jin, A.Rummel, T.Binz, and A.T.Brunger (2006).
Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity.

Nature, 444, 1092-1095.

PDB code:

2nm1

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.