3efx

From Proteopedia

(Difference between revisions)

Revision as of 15:21, 1 November 2023

Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin, 1.9A crystal structure reveals the details

Structural highlights

3efx is a 10 chain structure with sequence from Vibrio cholerae. This structure supersedes the now removed PDB entries 2nzg and 1tl0. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.94Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ELBH_ECOLX The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.CHTB_VIBCH The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself.

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

A hybrid between the B subunits of cholera toxin and Escherichia coli heat-labile enterotoxin has been described, which exhibits a novel binding specificity to blood group A and B type 2 determinants. In the present investigation, we have determined the crystal structure of this protein hybrid, termed LCTBK, in complex with the blood group A pentasaccharide GalNAcalpha3(Fucalpha2)Galbeta4(Fucalpha3)GlcNAcbeta, confirming not only the novel binding specificity but also a distinct new oligosaccharide binding site. Binding studies revealed that the new specificity can be ascribed to a single mutation (S4N) introduced into the sequence of Escherichia coli heat-labile enterotoxin. At a resolution of 1.9 A, the new binding site is resolved in excellent detail. Main features include a complex network of water molecules, which is well preserved by the parent toxins, and an unexpectedly modest contribution to binding by the critical residue Asn4, which interacts with the ligand only via a single water molecule.

Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin: 1.9 A crystal structure reveals the details.,Holmner A, Lebens M, Teneberg S, Angstrom J, Okvist M, Krengel U Structure. 2004 Sep;12(9):1655-67. PMID:15341730^[1]

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

References

↑ Holmner A, Lebens M, Teneberg S, Angstrom J, Okvist M, Krengel U. Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin: 1.9 A crystal structure reveals the details. Structure. 2004 Sep;12(9):1655-67. PMID:15341730 doi:10.1016/j.str.2004.06.022

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/3efx"

@@ Line 3: / Line 3: @@
 <StructureSection load='3efx' size='340' side='right'caption='[[3efx]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3efx]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2nzg 2nzg] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tl0 1tl0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EFX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3efx]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2nzg 2nzg] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tl0 1tl0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EFX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=3efx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3efx OCA], [https://pdbe.org/3efx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3efx RCSB], [https://www.ebi.ac.uk/pdbsum/3efx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3efx ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ELBH_ECOLX ELBH_ECOLX] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.[https://www.uniprot.org/uniprot/CHTB_VIBCH CHTB_VIBCH] The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
 [[Category: Large Structures]]
-[[Category: Angstrom, J]]
+[[Category: Vibrio cholerae]]
-[[Category: Holmner, A]]
+[[Category: Angstrom J]]
-[[Category: Krengel, U]]
+[[Category: Holmner A]]
-[[Category: Lebens, M]]
+[[Category: Krengel U]]
-[[Category: Okvist, M]]
+[[Category: Lebens M]]
-[[Category: Teneberg, S]]
+[[Category: Okvist M]]
-[[Category: Blood group antigen]]
+[[Category: Teneberg S]]
-[[Category: Cholera toxin]]
-[[Category: Heat-labile enterotoxin]]
-[[Category: Protein-carbohydrate complex]]
-[[Category: Toxin]]

3efx

From Proteopedia

Revision as of 15:21, 1 November 2023

Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin, 1.9A crystal structure reveals the details

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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