1bcp

From Proteopedia

(Difference between revisions)

Revision as of 05:59, 25 December 2014

BINARY COMPLEX OF PERTUSSIS TOXIN AND ATP

Structural highlights

1bcp is a 12 chain structure with sequence from Bordetella pertussis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[TOX4_BORPE] PTX oligomer B binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane. [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. [TOX3_BORPE] PTX oligomer B binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane. [TOX2_BORPE] PTX oligomer B binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane. [TOX5_BORPE] PTX oligomer B binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hazes B, Boodhoo A, Cockle SA, Read RJ. Crystal structure of the pertussis toxin-ATP complex: a molecular sensor. J Mol Biol. 1996 May 17;258(4):661-71. PMID:8637000 doi:10.1006/jmbi.1996.0277

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bcp"

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bcp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bcp RCSB], [http://www.ebi.ac.uk/pdbsum/1bcp PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/TOX4_BORPE TOX4_BORPE]] PTX oligomer B binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane. [[http://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. [[http://www.uniprot.org/uniprot/TOX3_BORPE TOX3_BORPE]] PTX oligomer B binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane. [[http://www.uniprot.org/uniprot/TOX2_BORPE TOX2_BORPE]] PTX oligomer B binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane. [[http://www.uniprot.org/uniprot/TOX5_BORPE TOX5_BORPE]] PTX oligomer B binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1bcp

From Proteopedia

Revision as of 05:59, 25 December 2014

BINARY COMPLEX OF PERTUSSIS TOXIN AND ATP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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