|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | [[Image:2ehn.jpg|left|200px]] | + | #REDIRECT [[3ah4]] This PDB entry is obsolete and replaced by 3ah4 |
| - | | + | |
| - | <!--
| + | |
| - | The line below this paragraph, containing "STRUCTURE_2ehn", creates the "Structure Box" on the page.
| + | |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | |
| - | or leave the SCENE parameter empty for the default display.
| + | |
| - | -->
| + | |
| - | {{STRUCTURE_2ehn| PDB=2ehn | SCENE= }}
| + | |
| - | | + | |
| - | '''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 [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==
| + | |
| - | 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: Single protein]]
| + | |
| - | [[Category: Ide, A.]]
| + | |
| - | [[Category: Nakamura, T.]]
| + | |
| - | [[Category: Nishikawa, A.]]
| + | |
| - | [[Category: Oguma, K.]]
| + | |
| - | [[Category: Tonozuka, T.]]
| + | |
| - | [[Category: Yuzawa, T.]]
| + | |
| - | [[Category: Beta trefoil]]
| + | |
| - | [[Category: Toxin]]
| + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:34:09 2008''
| + | |