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2j3v

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[[Image:2j3v.gif|left|200px]]<br />
 
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<applet load="2j3v" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2j3v, resolution 2.11&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE ENZYMATIC COMPONENT C2-I OF THE C2-TOXIN FROM CLOSTRIDIUM BOTULINUM AT PH 3.0'''<br />
 
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==Overview==
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==Crystal structure of the enzymatic component C2-I of the C2-toxin from Clostridium botulinum at pH 3.0==
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C2 toxin from Clostridium botulinum is composed of the enzyme component, C2-I, which ADP-ribosylates actin, and the binding and translocation, component C2-II, responsible for the interaction with eukaryotic cell, receptors and the following endocytosis. Three C2-I crystal structures at, resolutions of up to 1.75 A are presented together with a crystal, structure of C2-II at an appreciably lower resolution and a model of the, prepore formed by fragment C2-IIa. The C2-I structure was determined at pH, 3.0 and at pH 6.1. The structural differences are small, indicating that, C2-I does not unfold, even at a pH value as low as 3.0. The ADP-ribosyl, transferase activity of C2-I was determined for alpha and beta/gamma-actin, and related to that of Iota toxin and of mutant S361R of C2-I that, introduced the arginine observed in Iota toxin. The substantial activity, differences between alpha and beta/gamma-actin cannot be explained by the, protein structures currently available. The structure of the transport, component C2-II at pH 4.3 was established by molecular replacement using a, model of the protective antigen of anthrax toxin at pH 6.0. The C-terminal, receptor-binding domain of C2-II could not be located but was present in, the crystals. It may be mobile. The relative orientation and positions of, the four other domains of C2-II do not differ much from those of the, protective antigen, indicating that no large conformational changes occur, between pH 4.3 and pH 6.0. A model of the C2-IIa prepore structure was, constructed based on the corresponding assembly of the protective antigen., It revealed a surprisingly large number of asparagine residues lining the, pore. The interaction between C2-I and C2-IIa and the translocation of, C2-I into the target cell are discussed.
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<StructureSection load='2j3v' size='340' side='right'caption='[[2j3v]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2j3v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J3V 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]] 2.11&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2j3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j3v OCA], [https://pdbe.org/2j3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j3v RCSB], [https://www.ebi.ac.uk/pdbsum/2j3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j3v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O69275_CLOBO O69275_CLOBO]
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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/j3/2j3v_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=2j3v ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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C2 toxin from Clostridium botulinum is composed of the enzyme component C2-I, which ADP-ribosylates actin, and the binding and translocation component C2-II, responsible for the interaction with eukaryotic cell receptors and the following endocytosis. Three C2-I crystal structures at resolutions of up to 1.75 A are presented together with a crystal structure of C2-II at an appreciably lower resolution and a model of the prepore formed by fragment C2-IIa. The C2-I structure was determined at pH 3.0 and at pH 6.1. The structural differences are small, indicating that C2-I does not unfold, even at a pH value as low as 3.0. The ADP-ribosyl transferase activity of C2-I was determined for alpha and beta/gamma-actin and related to that of Iota toxin and of mutant S361R of C2-I that introduced the arginine observed in Iota toxin. The substantial activity differences between alpha and beta/gamma-actin cannot be explained by the protein structures currently available. The structure of the transport component C2-II at pH 4.3 was established by molecular replacement using a model of the protective antigen of anthrax toxin at pH 6.0. The C-terminal receptor-binding domain of C2-II could not be located but was present in the crystals. It may be mobile. The relative orientation and positions of the four other domains of C2-II do not differ much from those of the protective antigen, indicating that no large conformational changes occur between pH 4.3 and pH 6.0. A model of the C2-IIa prepore structure was constructed based on the corresponding assembly of the protective antigen. It revealed a surprisingly large number of asparagine residues lining the pore. The interaction between C2-I and C2-IIa and the translocation of C2-I into the target cell are discussed.
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==About this Structure==
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Structure and action of the binary C2 toxin from Clostridium botulinum.,Schleberger C, Hochmann H, Barth H, Aktories K, Schulz GE J Mol Biol. 2006 Dec 8;364(4):705-15. Epub 2006 Sep 5. PMID:17027031<ref>PMID:17027031</ref>
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2J3V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] with SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J3V OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure and action of the binary C2 toxin from Clostridium botulinum., Schleberger C, Hochmann H, Barth H, Aktories K, Schulz GE, J Mol Biol. 2006 Dec 8;364(4):705-15. Epub 2006 Sep 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17027031 17027031]
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</div>
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<div class="pdbe-citations 2j3v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Aktories, K.]]
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[[Category: Aktories K]]
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[[Category: Barth, H.]]
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[[Category: Barth H]]
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[[Category: Hochmann, H.]]
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[[Category: Hochmann H]]
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[[Category: Schleberger, C.]]
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[[Category: Schleberger C]]
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[[Category: Schulz, G.E.]]
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[[Category: Schulz GE]]
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[[Category: GOL]]
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[[Category: SO4]]
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[[Category: adp-ribosyltransferase]]
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[[Category: clostridium botulinum]]
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[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:07:57 2007''
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Current revision

Crystal structure of the enzymatic component C2-I of the C2-toxin from Clostridium botulinum at pH 3.0

PDB ID 2j3v

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