1qxm: Difference between revisions

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<StructureSection load='1qxm' size='340' side='right'caption='[[1qxm]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1qxm' size='340' side='right'caption='[[1qxm]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qxm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_c3 Bacteriophage c3]. 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>
<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='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>
</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>
<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>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HA33_CLOBO HA33_CLOBO]] 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.  
[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 ==
== 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=1qxm 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=1qxm ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Botulism food poisoning is caused primarily by ingestion of the Clostridium botulinum neurotoxin (BoNT). The 1300 amino acid BoNT forms a progenitor toxin (PTX) that, when associated with a number of other proteins, increases its oral toxicity by protecting it from the low pH of the stomach and from intestinal proteases. One of these associated proteins, HA1, has also been suggested to be involved with internalization of the toxin into the bloodstream by binding to oligosaccharides lining the intestine. Here is reported the crystal structure of HA1 from type C Clostridium botulinum at a resolution of 1.7 Angstrom. The protein consists of two beta-trefoil domains and bears structural similarities to the lectin B-chain from the deadly plant toxin ricin. Based on structural comparison to the ricin B-chain lactose-binding sites, residues of type A HA1 were selected and mutated. The D263A and N285A mutants lost the ability to bind carbohydrates containing galactose moieties, implicating these residues in carbohydrate binding.
Structural analysis by X-ray crystallography and calorimetry of a haemagglutinin component (HA1) of the progenitor toxin from Clostridium botulinum.,Inoue K, Sobhany M, Transue TR, Oguma K, Pedersen LC, Negishi M Microbiology. 2003 Dec;149(Pt 12):3361-70. PMID:14663070<ref>PMID:14663070</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1qxm" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacteriophage c3]]
[[Category: Clostridium botulinum D phage]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Inoue, K]]
[[Category: Inoue K]]
[[Category: Negishi, M]]
[[Category: Negishi M]]
[[Category: Oguma, K]]
[[Category: Oguma K]]
[[Category: Pedersen, L C]]
[[Category: Pedersen LC]]
[[Category: Sobhany, M]]
[[Category: Sobhany M]]
[[Category: Transue, T R]]
[[Category: Transue TR]]
[[Category: Clostridium botulinum]]
[[Category: Ha1]]
[[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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