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{{STRUCTURE_1qxm|  PDB=1qxm  |  SCENE=  }}
===Crystal structure of a hemagglutinin component (HA1) from type C Clostridium botulinum===
{{ABSTRACT_PUBMED_14663070}}


==About this Structure==
==Crystal structure of a hemagglutinin component (HA1) from type C Clostridium botulinum==
[[1qxm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum_d_phage Clostridium botulinum d phage]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXM OCA].  
<StructureSection load='1qxm' size='340' side='right'caption='[[1qxm]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qxm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum_D_phage Clostridium botulinum D phage]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QXM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=1qxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qxm OCA], [https://pdbe.org/1qxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qxm RCSB], [https://www.ebi.ac.uk/pdbsum/1qxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qxm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA33D_CBDP HA33D_CBDP] The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of the neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host. Involved in binding to the small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties (By similarity). Erythrocyte agglutination only occurs when the entire complex is assembled (PubMed:17581814). Binds eukaryotic host mucins as well as N-acetyl-beta-neuraminic acid, N-acetyl-D-galactosamine and galactose (but not glucose) via 2 sites (By similarity).[UniProtKB:P0DPR0]<ref>PMID:17581814</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qx/1qxm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1qxm ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Hemagglutinin|Hemagglutinin]]
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:014663070</ref><ref group="xtra">PMID:017009862</ref><references group="xtra"/>
__TOC__
[[Category: Clostridium botulinum d phage]]
</StructureSection>
[[Category: Inoue, K.]]
[[Category: Clostridium botulinum D phage]]
[[Category: Negishi, M.]]
[[Category: Large Structures]]
[[Category: Oguma, K.]]
[[Category: Inoue K]]
[[Category: Pedersen, L C.]]
[[Category: Negishi M]]
[[Category: Sobhany, M.]]
[[Category: Oguma K]]
[[Category: Transue, T R.]]
[[Category: Pedersen LC]]
[[Category: Clostridium botulinum]]
[[Category: Sobhany M]]
[[Category: Ha1]]
[[Category: Transue TR]]
[[Category: Hemagglutinin]]
[[Category: Toxin]]
[[Category: Trefoil]]

Latest revision as of 11:18, 14 February 2024

Crystal structure of a hemagglutinin component (HA1) from type C Clostridium botulinumCrystal structure of a hemagglutinin component (HA1) from type C Clostridium botulinum

Structural highlights

1qxm is a 2 chain structure with sequence from Clostridium botulinum D phage. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HA33D_CBDP The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of the neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host. Involved in binding to the small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties (By similarity). Erythrocyte agglutination only occurs when the entire complex is assembled (PubMed:17581814). Binds eukaryotic host mucins as well as N-acetyl-beta-neuraminic acid, N-acetyl-D-galactosamine and galactose (but not glucose) via 2 sites (By similarity).[UniProtKB:P0DPR0][1]

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. Hasegawa K, Watanabe T, Suzuki T, Yamano A, Oikawa T, Sato Y, Kouguchi H, Yoneyama T, Niwa K, Ikeda T, Ohyama T. A novel subunit structure of Clostridium botulinum serotype D toxin complex with three extended arms. J Biol Chem. 2007 Aug 24;282(34):24777-83. Epub 2007 Jun 20. PMID:17581814 doi:10.1074/jbc.M703446200

1qxm, resolution 1.70Å

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