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1tii

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Revision as of 11:27, 11 September 2015

ESCHERICHIA COLI HEAT LABILE ENTEROTOXIN TYPE IIB

Structural highlights

1tii is a 7 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[E2BB_ECOLX] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. [E2BA_ECOLX] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.

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

BACKGROUND: Cholera toxin from Vibrio cholerae and the type I heat-labile enterotoxins (LT-Is) from Escherichia coli are oligomeric proteins with AB5 structures. The type II heat-labile enterotoxins (LT-IIs) from E. coli are structurally similar to, but antigenically distinct from, the type I enterotoxins. The A subunits of type I and type II enterotoxins are homologous and activate adenylate cyclase by ADP-ribosylation of a G protein subunit, G8 alpha. However, the B subunits of type I and type II enterotoxins differ dramatically in amino acid sequence and ganglioside-binding specificity. The structure of LT-IIb was determined both as a prototype for other LT-IIs and to provide additional insights into structure/function relationships among members of the heat-labile enterotoxin family and the superfamily of ADP-ribosylating protein toxins. RESULTS: The 2.25 A crystal structure of the LT-IIb holotoxin has been determined. The structure reveals striking similarities with LT-I in both the catalytic A subunit and the ganglioside-binding B subunits. The latter form a pentamer which has a central pore with a diameter of 10-18 A. Despite their similarities, the relative orientation between the A polypeptide and the B pentamer differs by 24 degrees in LT-I and LT-IIb. A common hydrophobic ring was observed at the A-B5 interface which may be important in the cholera toxin family for assembly of the AB5 heterohexamer. A cluster of arginine residues at the surface of the A subunit of LT-I and cholera toxin, possibly involved in assembly, is also present in LT-IIb. The ganglioside receptor binding sites are localized, as suggested by mutagenesis, and are in a position roughly similar to the sites where LT-I binds its receptor. CONCLUSIONS: The structure of LT-IIb provides insight into the sequence diversity and structural similarity of the AB5 toxin family. New knowledge has been gained regarding the assembly of AB5 toxins and their active-site architecture.

Crystal structure of a new heat-labile enterotoxin, LT-IIb.,van den Akker F, Sarfaty S, Twiddy EM, Connell TD, Holmes RK, Hol WG Structure. 1996 Jun 15;4(6):665-78. PMID:8805549^[1]

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

References

↑ van den Akker F, Sarfaty S, Twiddy EM, Connell TD, Holmes RK, Hol WG. Crystal structure of a new heat-labile enterotoxin, LT-IIb. Structure. 1996 Jun 15;4(6):665-78. PMID:8805549

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 2: / Line 2: @@
 <StructureSection load='1tii' size='340' side='right' caption='[[1tii]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1tii]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TII OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TII FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1tii]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TII OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TII FirstGlance]. <br>
-</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=1tii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tii OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tii RCSB], [http://www.ebi.ac.uk/pdbsum/1tii PDBsum]</span></td></tr>
+</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=1tii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tii OCA], [http://pdbe.org/1tii PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tii RCSB], [http://www.ebi.ac.uk/pdbsum/1tii PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/E2BB_ECOLI E2BB_ECOLI]] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. [[http://www.uniprot.org/uniprot/E2BA_ECOLI E2BA_ECOLI]] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
+[[http://www.uniprot.org/uniprot/E2BB_ECOLX E2BB_ECOLX]] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. [[http://www.uniprot.org/uniprot/E2BA_ECOLX E2BA_ECOLX]] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1tii" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Bacillus coli migula 1895]]
 [[Category: Akker, F Van Den]]
 [[Category: Hol, W G.J]]

1tii

From Proteopedia

Revision as of 11:27, 11 September 2015

ESCHERICHIA COLI HEAT LABILE ENTEROTOXIN TYPE IIB

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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