1FV2

The Hc fragment of tetanus toxin complexed with an analogue of its ganglioside receptor GT1B

Summary for 1FV2

• Entry DOI: 10.2210/pdb1fv2/pdb
• Related: 1a8d 1af9 1d0h 1dfq 1diw 1dll 1fv3
• Descriptor: TETANUS TOXIN HEAVY CHAIN, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-8)-N-acetyl-beta-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: toxin, carbohydrate, ganglioside, multi-valent binding, receptor
• Biological source: Clostridium tetani
• Total number of polymer chains: 1
• Total formula weight: 55776.39

Authors

Fotinou, C.,Emsley, P.,Black, I.,Ando, H.,Ishida, H.,Kiso, M.,Sinha, K.A.,Fairweather, N.F.,Isaacs, N.W. (deposition date: 2000-09-18, release date: 2001-09-05, Last modification date: 2024-11-20)

Primary citation

Fotinou, C.,Emsley, P.,Black, I.,Ando, H.,Ishida, H.,Kiso, M.,Sinha, K.A.,Fairweather, N.F.,Isaacs, N.W.
The crystal structure of tetanus toxin Hc fragment complexed with a synthetic GT1b analogue suggests cross-linking between ganglioside receptors and the toxin.
J.Biol.Chem., 276:32274-32281, 2001

PubMed Abstract: Tetanus toxin, a member of the family of Clostridial neurotoxins, is one of the most potent toxins known. The crystal structure of the complex of the COOH-terminal fragment of the heavy chain with an analogue of its ganglioside receptor, GT1b, provides the first direct identification and characterization of the ganglioside-binding sites. The ganglioside induces cross-linking by binding to two distinct sites on the Hc molecule. The structure sheds new light on the binding of Clostridial neurotoxins to receptors on neuronal cells and provides important information relevant to the design of anti-tetanus and anti-botulism therapeutic agents.

PubMed: 11418600
DOI: 10.1074/jbc.M103285200

Experimental method

X-RAY DIFFRACTION (2.5 Å)