1qxm
From Proteopedia
(New page: 200px<br /><applet load="1qxm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qxm, resolution 1.70Å" /> '''Crystal structure of...) |
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| - | [[Image:1qxm.gif|left|200px]]<br /><applet load="1qxm" size=" | + | [[Image:1qxm.gif|left|200px]]<br /><applet load="1qxm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qxm, resolution 1.70Å" /> | caption="1qxm, resolution 1.70Å" /> | ||
'''Crystal structure of a hemagglutinin component (HA1) from type C Clostridium botulinum'''<br /> | '''Crystal structure of a hemagglutinin component (HA1) from type C Clostridium botulinum'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Botulism food poisoning is caused primarily by ingestion of the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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 EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Negishi, M.]] | [[Category: Negishi, M.]] | ||
[[Category: Oguma, K.]] | [[Category: Oguma, K.]] | ||
| - | [[Category: Pedersen, L | + | [[Category: Pedersen, L C.]] |
[[Category: Sobhany, M.]] | [[Category: Sobhany, M.]] | ||
| - | [[Category: Transue, T | + | [[Category: Transue, T R.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: clostridium botulinum]] | [[Category: clostridium botulinum]] | ||
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[[Category: trefoil]] | [[Category: trefoil]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:48 2008'' |
Revision as of 12:44, 21 February 2008
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Crystal structure of a hemagglutinin component (HA1) from type C Clostridium botulinum
Overview
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.
About this Structure
1QXM is a Single protein structure of sequence from Clostridium botulinum d phage with as ligand. Full crystallographic information is available from OCA.
Reference
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
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