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2wv6

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Current revision

Crystal structure of the cholera toxin-like B-subunit from Citrobacter freundii to 1.9 angstrom

Structural highlights

2wv6 is a 10 chain structure with sequence from Citrobacter freundii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.895Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8GAV5_CITFR

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

Enterotoxigenic Escherichia coli and Vibrio cholerae are well known causative agents of severe diarrheal diseases. Both pathogens produce AB(5) toxins, with one enzymatically active A-subunit and a pentamer of receptor-binding B-subunits. The primary receptor for both B-subunits is the GM1 ganglioside (Galbeta3GalNAcbeta4(NeuAcalpha3)Galbeta4GlcbetaCer), but the B-subunits from porcine isolates of E. coli also bind neolacto-(Galbeta4GlcNAcbeta-)terminated glycoconjugates and the B-subunits from human isolates of E. coli (hLTB) have affinity for blood group A type 2-(GalNAcalpha3(Fucalpha2)Galbeta4GlcNAcbeta-)terminated glycoconjugates. A B-subunit with 73% sequence identity to the B-subunits of cholera toxin and the heat-labile toxin of E. coli is produced by certain strains of enteropathogenic E. coli and by Citrobacter freundii. This C. freundii B-subunit (CFXB) has now been expressed in V. cholerae, and isolated in high yields. Glycosphingolipid binding studies show that CFXB binds to the GM1 ganglioside with high affinity. In addition, CFXB has high affinity for both neolacto-terminated and blood group A type 2-terminated glycoconjugates. The crystal structure of the pentameric arrangement of C. freundii B-subunits display high structural similarity with related proteins from E. coli and V. cholerae and oligosaccharide binding sites can be identified on the protein surface. Small changes in the 88-95 loop connecting the GM1 and blood group A binding sites explains the minor changes in affinity seen for these two ligands. However, the enhanced affinity of CFXB for neolacto-terminated structures can be sought in the Lys34Tyr substitution affording additional hydrogen bond interactions between the tyrosyl side chain and the GlcNAcbeta3Galb4Glcbeta1 segment of neolactotetraosylceramide via bridging water molecules.

Carbohydrate binding specificities and crystal structure of the cholera toxin-like B-subunit from Citrobacter freundii.,Jansson L, Angstrom J, Lebens M, Imberty A, Varrot A, Teneberg S Biochimie. 2010 May;92(5):482-90. Epub 2010 Feb 18. PMID:20171259^[1]

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

References

↑ Jansson L, Angstrom J, Lebens M, Imberty A, Varrot A, Teneberg S. Carbohydrate binding specificities and crystal structure of the cholera toxin-like B-subunit from Citrobacter freundii. Biochimie. 2010 May;92(5):482-90. Epub 2010 Feb 18. PMID:20171259 doi:10.1016/j.biochi.2010.02.010

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/2wv6"

@@ Line 3: / Line 3: @@
 <StructureSection load='2wv6' size='340' side='right'caption='[[2wv6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wv6]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_freundii"_braak_1928 "bacterium freundii" braak 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WV6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wv6]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WV6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.895&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2wv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wv6 OCA], [https://pdbe.org/2wv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wv6 RCSB], [https://www.ebi.ac.uk/pdbsum/2wv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wv6 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q8GAV5_CITFR Q8GAV5_CITFR]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacterium freundii braak 1928]]
+[[Category: Citrobacter freundii]]
 [[Category: Large Structures]]
-[[Category: Imberty, A]]
+[[Category: Imberty A]]
-[[Category: Jansson, L]]
+[[Category: Jansson L]]
-[[Category: Lebens, M]]
+[[Category: Lebens M]]
-[[Category: Teneberg, S]]
+[[Category: Teneberg S]]
-[[Category: Varrot, A]]
+[[Category: Varrot A]]
-[[Category: B subunit]]
-[[Category: Cholera toxin-like]]
-[[Category: Lectin]]
-[[Category: Toxin]]

2wv6

From Proteopedia

Current revision

Crystal structure of the cholera toxin-like B-subunit from Citrobacter freundii to 1.9 angstrom

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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