1Z0H

N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B

Summary for 1Z0H

• Entry DOI: 10.2210/pdb1z0h/pdb
• Related: 1ERW
• Descriptor: Botulinum neurotoxin type B (2 entities in total)
• Functional Keywords: clostridium botulinum, binding domain, gangliosides, hydrolase
• Biological source: Clostridium botulinum
• Cellular location: Botulinum neurotoxin B light chain: Secreted. Botulinum neurotoxin B heavy chain: Secreted: P10844
• Total number of polymer chains: 2
• Total formula weight: 105460.65

Authors

Jayaraman, S.,Eswarmoorthy, S.,Ashraf, S.A.,Smith, L.A.,Swaminathan, S. (deposition date: 2005-03-01, release date: 2005-03-15, Last modification date: 2023-08-23)

Primary citation

Jayaraman, S.,Eswaramoorthy, S.,Ahmed, S.A.,Smith, L.A.,Swaminathan, S.
N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B.
Biochem.Biophys.Res.Commun., 330:97-103, 2005

PubMed 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.

PubMed: 15781237
DOI: 10.1016/j.bbrc.2005.02.123

Experimental method

X-RAY DIFFRACTION (2 Å)