1qxm

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[[Image:1qxm.gif|left|200px]]<br /><applet load="1qxm" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qxm, resolution 1.70&Aring;" />
 
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'''Crystal structure of a hemagglutinin component (HA1) from type C Clostridium botulinum'''<br />
 
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==Overview==
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==Crystal structure of a hemagglutinin component (HA1) from type C Clostridium botulinum==
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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.
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<StructureSection load='1qxm' size='340' side='right'caption='[[1qxm]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qx/1qxm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1QXM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum_d_phage Clostridium botulinum d phage] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QXM OCA].
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
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== References ==
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==Reference==
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<references/>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14663070 14663070]
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__TOC__
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[[Category: Clostridium botulinum d phage]]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Clostridium botulinum D phage]]
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[[Category: Inoue, K.]]
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[[Category: Large Structures]]
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[[Category: Negishi, M.]]
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[[Category: Inoue K]]
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[[Category: Oguma, K.]]
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[[Category: Negishi M]]
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[[Category: Pedersen, L C.]]
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[[Category: Oguma K]]
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[[Category: Sobhany, M.]]
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[[Category: Pedersen LC]]
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[[Category: Transue, T R.]]
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[[Category: Sobhany M]]
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[[Category: EDO]]
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[[Category: Transue TR]]
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[[Category: clostridium botulinum]]
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[[Category: ha1]]
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[[Category: hemagglutinin]]
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[[Category: trefoil]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:48 2008''
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Current revision

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

PDB ID 1qxm

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