1bcp

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[[Image:1bcp.png|left|200px]]
 
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==BINARY COMPLEX OF PERTUSSIS TOXIN AND ATP==
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The line below this paragraph, containing "STRUCTURE_1bcp", creates the "Structure Box" on the page.
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<StructureSection load='1bcp' size='340' side='right'caption='[[1bcp]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1bcp]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BCP 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]] 2.7&#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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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{{STRUCTURE_1bcp| PDB=1bcp | SCENE= }}
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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=1bcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bcp OCA], [https://pdbe.org/1bcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bcp RCSB], [https://www.ebi.ac.uk/pdbsum/1bcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bcp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TOX1_BORPE TOX1_BORPE] S1 is an NAD-dependent ADP-ribosyltransferase, which plays a crucial role in the pathogenesis of B.pertussis causing disruption of normal host cellular regulation. It catalyzes the ADP-ribosylation of a cysteine in the alpha subunit of host heterotrimeric G proteins. In the absence of G proteins it also catalyzes the cleavage of NAD(+) into ADP-ribose and nicotinamide. It irreversibly uncouples the G-alpha GTP-binding proteins from their membrane receptors.
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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/bc/1bcp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1bcp 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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Pertussis toxin is a major virulence factor of Bordetella pertussis, the causative agent of whooping cough. The protein is a hexamer containing a catalytic subunit (S1) that is tightly associated with a pentameric cell-binding component (B-oligomer). In vitro experiments have shown that ATP and a number of detergents and phospholipids assist in activating the holotoxin by destabilizing the interaction between S1 and the B-oligomer. Similar processes may play a role in the activation of pertussis toxin in vivo. In this paper we present the crystal structure of the pertussis toxin-ATP complex and discuss the structural basis for the ATP-induced activation. In addition, we propose a physiological role for the ATP effect in the process by which the toxin enters the cytoplasm of eukaryotic cells. The key features of this proposal are that ATP binding signals the arrival of the toxin in the endoplasmic reticulum and, at the same time, triggers dissociation of the holotoxin prior to membrane translocation.
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===BINARY COMPLEX OF PERTUSSIS TOXIN AND ATP===
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Crystal structure of the pertussis toxin-ATP complex: a molecular sensor.,Hazes B, Boodhoo A, Cockle SA, Read RJ J Mol Biol. 1996 May 17;258(4):661-71. PMID:8637000<ref>PMID:8637000</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1bcp" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_8637000}}, adds the Publication Abstract to the page
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*[[Pertussis toxin|Pertussis toxin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 8637000 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_8637000}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1BCP is a 12 chains structure of sequences from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCP OCA].
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==Reference==
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<ref group="xtra">PMID:8637000</ref><references group="xtra"/>
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[[Category: Bordetella pertussis]]
[[Category: Bordetella pertussis]]
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[[Category: Hazes, B.]]
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[[Category: Large Structures]]
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[[Category: Read, R J.]]
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[[Category: Hazes B]]
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[[Category: Adp-ribosyltransferase]]
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[[Category: Read RJ]]
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[[Category: Toxin]]
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[[Category: Transferase]]
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[[Category: Whooping cough]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 08:44:45 2009''
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BINARY COMPLEX OF PERTUSSIS TOXIN AND ATP

PDB ID 1bcp

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