1z0h: Difference between revisions

Revision as of 10:14, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1z0h.png

Template:STRUCTURE 1z0h

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

Template:ABSTRACT PUBMED 15781237

About this StructureAbout this Structure

1Z0H is a Single protein structure of sequence from Clostridium botulinum. Full crystallographic information is available from OCA.

ReferenceReference

N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B., Jayaraman S, Eswaramoorthy S, Ahmed SA, Smith LA, Swaminathan S, Biochem Biophys Res Commun. 2005 Apr 29;330(1):97-103. PMID:15781237

Page seeded by OCA on Mon Jul 28 10:14:19 2008

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OCA

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-'''N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B'''
+===N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15781237}}, adds the Publication Abstract to the page
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 [[Category: Ganglioside]]
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