2ehn

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(New page: 200px<br /><applet load="2ehn" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ehn, resolution 1.78&Aring;" /> '''HA1 subcomponent of ...)
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[[Image:2ehn.jpg|left|200px]]<br /><applet load="2ehn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ehn.jpg|left|200px]]
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caption="2ehn, resolution 1.78&Aring;" />
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'''HA1 subcomponent of botulinum type C progenitor toxin complexed with galactose'''<br />
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{{Structure
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|PDB= 2ehn |SIZE=350|CAPTION= <scene name='initialview01'>2ehn</scene>, resolution 1.78&Aring;
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|SITE= <scene name='pdbsite=AC1:Gal+Binding+Site+For+Residue+B+2000'>AC1</scene> and <scene name='pdbsite=AC2:Gal+Binding+Site+For+Residue+B+2001'>AC2</scene>
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|LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''HA1 subcomponent of botulinum type C progenitor toxin complexed with galactose'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2EHN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] with <scene name='pdbligand=GAL:'>GAL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:Gal+Binding+Site+For+Residue+B+2000'>AC1</scene> and <scene name='pdbsite=AC2:Gal+Binding+Site+For+Residue+B+2001'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EHN OCA].
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2EHN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EHN OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=18178224 18178224]
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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]
[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:10:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:40:21 2008''

Revision as of 14:40, 20 March 2008

Image:2ehn.jpg


PDB ID 2ehn

Drag the structure with the mouse to rotate
, resolution 1.78Å
Sites: and
Ligands:
Coordinates: save as pdb, mmCIF, xml



HA1 subcomponent of botulinum type C progenitor toxin complexed with galactose


Overview

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.

About this Structure

2EHN is a Single protein structure of sequence from Clostridium botulinum. Full crystallographic information is available from OCA.

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:18178224

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