PDBsum entry: 1ybi

Toxin

PDB id: 1ybi

Contents

Protein chains

284 a.a. *

Waters ×564

* Residue conservation analysis

PDB id:

1ybi

Name:

Toxin

Title:

Crystal structure of ha33a, a neurotoxin-associated protein from clostridium botulinum type a

Structure:

Non-toxin haemagglutinin ha34. Chain: a, b. Synonym: ha33a, ha33/a

Source:

Clostridium botulinum. Organism_taxid: 1491. Strain: serotype a, hall strain

Resolution:

1.50Å R-factor: 0.169 R-free: 0.194

Authors:

J.W.Arndt,J.Gu,L.Jaroszewski,R.Schwarzenbacher,M.Hanson, F.J.Lebeda,R.C.Stevens

Key ref:

J.W.Arndt et al. (2005). The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring beta-trefoil fold in the progenitor toxin complex. J Mol Biol, 346, 1083-1093. PubMed id: 15701519 DOI: 10.1016/j.jmb.2004.12.039

Date:

20-Dec-04 Release date: 22-Feb-05

Protein chains

Q45871  (Q45871_CLOBO) -  HA-33

Seq: 293 a.a.

Struc: 284 a.a.

DOI no: 10.1016/j.jmb.2004.12.039

J Mol Biol 346:1083-1093 (2005)

PubMed id: 15701519

The structure of the neurotoxin-associated protein HA33/A from Clostridium botulinum suggests a reoccurring beta-trefoil fold in the progenitor toxin complex.

J.W.Arndt, J.Gu, L.Jaroszewski, R.Schwarzenbacher, M.A.Hanson, F.J.Lebeda, R.C.Stevens.

ABSTRACT

The hemagglutinating protein HA33 from Clostridium botulinum is associated with the large botulinum neurotoxin secreted complexes and is critical in toxin protection, internalization, and possibly activation. We report the crystal structure of serotype A HA33 (HA33/A) at 1.5 A resolution that contains a unique domain organization and a carbohydrate recognition site. In addition, sequence alignments of the other toxin complex components, including the neurotoxin BoNT/A, hemagglutinating protein HA17/A, and non-toxic non-hemagglutinating protein NTNHA/A, suggests that most of the toxin complex consists of a reoccurring beta-trefoil fold.

Selected figure(s)

Figure 2.
Figure 2. (a) Ribbon diagram of an N-terminal superposition of HA33/A chain A (red) and HA33/A chain B (green). (b) Same superposition as (a), but superposition of HA33/A chain A (red) and HA33/C (white). (c) Same superposition used above, but containing a close-up view of the helical linker region.

Figure 4.
Figure 4. (a) Close-up view of HA33/A super-posed on the ricin lactose-binding site at the 2g repeat region. Putative carbohydrate-binding residues as observed in HA33/A (slate blue) and their counterparts as found in the lactose-bound ricin structure (salmon). Residue labels are indicated for HA33/A with those from the ricin structure in parentheses. (b) Similar overlay as in (a), but a close-up view at the 2g repeat of HA33/A (slate blue) superposed on HA33/C (white), with a modeled lactose molecule (salmon) and with HA33/C labels in parentheses.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2005, 346, 1083-1093) copyright 2005.

Figures were selected by an automated process.