1pto

From Proteopedia

(Difference between revisions)

Revision as of 09:34, 8 September 2021

THE STRUCTURE OF A PERTUSSIS TOXIN-SUGAR COMPLEX AS A MODEL FOR RECEPTOR BINDING

Structural highlights

1pto 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:
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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. [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. [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. [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 an exotoxin from the bacterium Bordetella pertussis which is important the pathogenesis of whooping cough and the generation of a protective immune response. The diverse biological activities of the toxin depend on its ability to recognize carbohydrate-containing receptors on a wide variety of eukaryotic cells. We present here the crystal structure of pertussis toxin complexed with a soluble oligosaccharide from transferrin. Binding sites for the terminal sialic acid-galactose moiety are revealed on both subunits S2 and S3 of the B-oligomer. Identification of amino acid residues involved in receptor binding will improve the design of genetically inactivated toxins for use in new acellular whooping cough vaccines.

Structure of a pertussis toxin-sugar complex as a model for receptor binding.,Stein PE, Boodhoo A, Armstrong GD, Heerze LD, Cockle SA, Klein MH, Read RJ Nat Struct Biol. 1994 Sep;1(9):591-6. PMID:7634099^[1]

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

References

↑ Stein PE, Boodhoo A, Armstrong GD, Heerze LD, Cockle SA, Klein MH, Read RJ. Structure of a pertussis toxin-sugar complex as a model for receptor binding. Nat Struct Biol. 1994 Sep;1(9):591-6. PMID:7634099

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/1pto"

Categories: Bordetella pertussis | Large Structures | Read, R J | Stein, P E | Toxin

@@ Line 3: / Line 3: @@
 <StructureSection load='1pto' size='340' side='right'caption='[[1pto]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1pto]] is a 12 chain structure with sequence 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=1PTO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PTO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1pto]] 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=1PTO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PTO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr>
-<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=1pto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pto OCA], [http://pdbe.org/1pto PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pto RCSB], [http://www.ebi.ac.uk/pdbsum/1pto PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pto ProSAT]</span></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pto OCA], [https://pdbe.org/1pto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pto RCSB], [https://www.ebi.ac.uk/pdbsum/1pto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pto ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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/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/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/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.
+[[https://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. [[https://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. [[https://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. [[https://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]]

1pto

From Proteopedia

Revision as of 09:34, 8 September 2021

THE STRUCTURE OF A PERTUSSIS TOXIN-SUGAR COMPLEX AS A MODEL FOR RECEPTOR BINDING

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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