2zs6: Difference between revisions

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<StructureSection load='2zs6' size='340' side='right'caption='[[2zs6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='2zs6' size='340' side='right'caption='[[2zs6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2zs6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2z5a 2z5a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZS6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZS6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2zs6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2z5a 2z5a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZS6 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ehm|2ehm]], [[2ehn|2ehn]], [[2ehi|2ehi]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2zs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zs6 OCA], [http://pdbe.org/2zs6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zs6 RCSB], [http://www.ebi.ac.uk/pdbsum/2zs6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zs6 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zs6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zs6 OCA], [https://pdbe.org/2zs6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zs6 RCSB], [https://www.ebi.ac.uk/pdbsum/2zs6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zs6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA70C_CBCP HA70C_CBCP] The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of botulinum neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host (PubMed:9421908). The HA component is involved in binding to the upper small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties (Probable). Whole protein and the HA-53 chain (but not the HA-22-23 chain) bind to bovine mucin; if the mucin is pretreated with neuraminidase (removes the terminal sialic acid of glycoconjugates) mucin binding is decreased (PubMed:19071137). Has higher affinity for alpha-2,3-sialylated oligosaccharides than alpha-2-6 sialylated oligosaccharides (PubMed:22684008).<ref>PMID:19071137</ref> <ref>PMID:22684008</ref> <ref>PMID:9421908</ref> <ref>PMID:9421908</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zs6 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zs6 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Clostridium botulinum type C 16S progenitor toxin contains a neurotoxin and several nontoxic components, designated nontoxic nonhemagglutinin (HA), HA1 (HA-33), HA2 (HA-17), HA3a (HA-22-23), and HA3b (HA-53). The HA3b subcomponent seems to play an important role cooperatively with HA1 in the internalization of the toxin by gastrointestinal epithelial cells via binding of these subcomponents to specific oligosaccharides. In this study, we investigated the sugar-binding specificity of the HA3b subcomponent using recombinant protein fused to glutathione S-transferase and determined the three-dimensional structure of the HA3a-HA3b complex based on X-ray crystallography. The crystal structure was determined at a resolution of 2.6 A. HA3b contains three domains, domains I to III, and the structure of domain I resembles HA3a. In crystal packing, three HA3a-HA3b molecules are assembled to form a three-leaved propeller-like structure. The three HA3b domain I and three HA3a alternate, forming a trimer of dimers. In a database search, no proteins with high structural homology to any of the domains (Z score &gt;10) were found. Especially, HA3a and HA3b domain I, mainly composed of beta-sheets, reveal a unique fold. In binding assays, HA3b bound sialic acid with high affinity, but did not bind galactose, N-acetylgalactosamine, or N-acetylglucosamine. The electron density of liganded N-acetylneuraminic acid was determined by crystal soaking. In the sugar-complex structure, the N-acetylneuraminic acid-binding site was located in the cleft formed between domains II and III of HA3b. This report provides the first determination of the three-dimensional structure of the HA3a-HA3b complex and its sialic acid binding site. Our results will provide useful information for elucidating the mechanism of assembly of the C16S toxin and for understanding the interactions with oligosaccharides on epithelial cells and internalization of the botulinum toxin complex.
Crystal structure of the HA3 subcomponent of Clostridium botulinum type C progenitor toxin.,Nakamura T, Kotani M, Tonozuka T, Ide A, Oguma K, Nishikawa A J Mol Biol. 2009 Jan 30;385(4):1193-206. Epub 2008 Nov 27. PMID:19071137<ref>PMID:19071137</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2zs6" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus botulinus van ermengem 1896]]
[[Category: Clostridium botulinum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kotani, M]]
[[Category: Kotani M]]
[[Category: Nakamura, T]]
[[Category: Nakamura T]]
[[Category: Nishikawa, A]]
[[Category: Nishikawa A]]
[[Category: Oguma, K]]
[[Category: Oguma K]]
[[Category: Tonozuka, T]]
[[Category: Tonozuka T]]
[[Category: Botulinum toxin]]
[[Category: Hemagglutinin]]
[[Category: Lectin]]
[[Category: Toxin]]

Latest revision as of 16:58, 13 March 2024

HA3 subcomponent of botulinum type C progenitor toxinHA3 subcomponent of botulinum type C progenitor toxin

Structural highlights

2zs6 is a 2 chain structure with sequence from Clostridium botulinum. This structure supersedes the now removed PDB entry 2z5a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HA70C_CBCP The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of botulinum neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host (PubMed:9421908). The HA component is involved in binding to the upper small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties (Probable). Whole protein and the HA-53 chain (but not the HA-22-23 chain) bind to bovine mucin; if the mucin is pretreated with neuraminidase (removes the terminal sialic acid of glycoconjugates) mucin binding is decreased (PubMed:19071137). Has higher affinity for alpha-2,3-sialylated oligosaccharides than alpha-2-6 sialylated oligosaccharides (PubMed:22684008).[1] [2] [3] [4]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Nakamura T, Kotani M, Tonozuka T, Ide A, Oguma K, Nishikawa A. Crystal structure of the HA3 subcomponent of Clostridium botulinum type C progenitor toxin. J Mol Biol. 2009 Jan 30;385(4):1193-206. Epub 2008 Nov 27. PMID:19071137 doi:10.1016/j.jmb.2008.11.039
  2. ↑ Yamashita S, Yoshida H, Uchiyama N, Nakakita Y, Nakakita S, Tonozuka T, Oguma K, Nishikawa A, Kamitori S. Carbohydrate recognition mechanism of HA70 from Clostridium botulinum deduced from X-ray structures in complexes with sialylated oligosaccharides. FEBS Lett. 2012 Jul 30;586(16):2404-10. doi: 10.1016/j.febslet.2012.05.055. Epub , 2012 Jun 7. PMID:22684008 doi:10.1016/j.febslet.2012.05.055
  3. ↑ Fujinaga Y, Inoue K, Watanabe S, Yokota K, Hirai Y, Nagamachi E, Oguma K. The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of guinea pig small intestine, leading to the efficient absorption of the toxin. Microbiology (Reading). 1997 Dec;143 ( Pt 12):3841-3847. doi:, 10.1099/00221287-143-12-3841. PMID:9421908 doi:http://dx.doi.org/10.1099/00221287-143-12-3841
  4. ↑ Fujinaga Y, Inoue K, Watanabe S, Yokota K, Hirai Y, Nagamachi E, Oguma K. The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of guinea pig small intestine, leading to the efficient absorption of the toxin. Microbiology (Reading). 1997 Dec;143 ( Pt 12):3841-3847. doi:, 10.1099/00221287-143-12-3841. PMID:9421908 doi:http://dx.doi.org/10.1099/00221287-143-12-3841

2zs6, resolution 2.60Å

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