2ehi: Difference between revisions

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[[Image:2ehi.jpg|left|200px]]
{{Seed}}
[[Image:2ehi.png|left|200px]]


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{{STRUCTURE_2ehi|  PDB=2ehi  |  SCENE=  }}  
{{STRUCTURE_2ehi|  PDB=2ehi  |  SCENE=  }}  


'''HA1 subcomponent of botulinum type C progenitor toxin complexed with N-acetylneuramic acid'''
===HA1 subcomponent of botulinum type C progenitor toxin complexed with N-acetylneuramic acid===




==Overview==
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Clostridium botulinum type C 16S progenitor toxin contains a hemagglutinin (HA) subcomponent, designated HA1, which appears to play an important role in the effective internalization of the toxin in gastrointestinal epithelial cells and in creating a broad specificity for the oligosaccharide structure that corresponds to various targets. In this study, using the recombinant protein fused to glutathione S-transferase, we investigated the binding specificity of the HA1 subcomponent to sugars and estimated the binding sites of HA1 based on X-ray crystallography and soaking experiments using various sugars. N-Acetylneuraminic acid, N-acetylgalactosamine, and galactose effectively inhibited the binding that occurs between glutathione S-transferase-HA1 and mucins, whereas N-acetylglucosamine and glucose did not inhibit it. The crystal structures of HA1 complex with N-acetylneuraminic acid, N-acetylgalactosamine, and galactose were also determined. There are two sugar-binding sites, sites I and II. Site I corresponds to the electron densities noted for all sugars and is located at the C-terminal beta-trefoil domain, while site II corresponds to the electron densities noted only for galactose. An aromatic amino acid residue, Trp176, at site I has a stacking interaction with the hexose ring of the sugars. On the other hand, there is no aromatic residue at site II; thus, the interaction with galactose seems to be poor. The double mutant W176A at site I and D271F at site II has no avidity for N-acetylneuraminic acid but has avidity for galactose. In this report, the binding specificity of botulinum C16S toxin HA1 to various sugars is demonstrated based on its structural features.
The line below this paragraph, {{ABSTRACT_PUBMED_18178224}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18178224 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18178224}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Sugar-binding sites of the HA1 subcomponent of Clostridium botulinum type C progenitor toxin., Nakamura T, Tonozuka T, Ide A, Yuzawa T, Oguma K, Nishikawa A, J Mol Biol. 2008 Feb 22;376(3):854-67. Epub 2007 Dec 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18178224 18178224]
Sugar-binding sites of the HA1 subcomponent of Clostridium botulinum type C progenitor toxin., Nakamura T, Tonozuka T, Ide A, Yuzawa T, Oguma K, Nishikawa A, J Mol Biol. 2008 Feb 22;376(3):854-67. Epub 2007 Dec 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18178224 18178224]
Binding properties of Clostridium botulinum type C progenitor toxin to mucins., Nakamura T, Takada N, Tonozuka T, Sakano Y, Oguma K, Nishikawa A, Biochim Biophys Acta. 2007 Apr;1770(4):551-5. Epub 2006 Nov 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17196748 17196748]
Cell internalization and traffic pathway of Clostridium botulinum type C neurotoxin in HT-29 cells., Uotsu N, Nishikawa A, Watanabe T, Ohyama T, Tonozuka T, Sakano Y, Oguma K, Biochim Biophys Acta. 2006 Jan;1763(1):120-8. Epub 2005 Dec 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16413070 16413070]
[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Beta trefoil]]
[[Category: Beta trefoil]]
[[Category: Toxin]]
[[Category: Toxin]]
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