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2x2t

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CRYSTAL STRUCTURE OF SCLEROTINIA SCLEROTIORUM AGGLUTININ SSA in complex with Gal-beta1,3-Galnac

Structural highlights

2x2t is a 1 chain structure with sequence from Sclerotinia sclerotiorum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.97Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AGGL_SCLSC Lectin that primarily recognizes glycans with a non-reducing terminal N-acetylgalactosamine (GalNAc), with a preference for the alpha- over the beta-anomer. Can also bind non-reducing terminal galactose (Gal) residues but with a lower affinity. Strongly interacts with glycolipid type glycans with terminal non-reducing Gal or GalNAc but fails to bind sialylated or fucosylated forms of the same glycans. Strongly interacts with galactosylated N-glycans, displaying highest affinity for alpha-1-3 branched mono-antennary N-glycans but also binding to multi-antennary glycans.^[1] ^[2] ^[3]

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 lectin from the phytopathogenic ascomycete Sclerotinia sclerotiorum that shares only weak sequence similarity with characterized fungal lectins has recently been identified. S. sclerotiorum agglutinin (SSA) is a homodimeric protein consisting of two identical subunits of approximately 17 kDa and displays specificity primarily towards Gal/GalNAc. Glycan array screening indicates that SSA readily interacts with Gal/GalNAc-bearing glycan chains. The crystal structures of SSA in the ligand-free form and in complex with the Gal-beta1,3-GalNAc (T-antigen) disaccharide have been determined at 1.6 and 1.97 A resolution, respectively. SSA adopts a beta-trefoil domain as previously identified for other carbohydrate-binding proteins of the ricin B-like lectin superfamily and accommodates terminal non-reducing galactosyl and N-acetylgalactosaminyl glycans. Unlike other structurally related lectins, SSA contains a single carbohydrate-binding site at site alpha. SSA reveals a novel dimeric assembly markedly dissimilar to those described earlier for ricin-type lectins. The present structure exemplifies the adaptability of the beta-trefoil domain in the evolution of fungal lectins.

Crystal structure of the GalNAc/Gal-specific agglutinin from the phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel adaptation of a beta-trefoil domain.,Sulzenbacher G, Roig-Zamboni V, Peumans WJ, Rouge P, Van Damme EJ, Bourne Y J Mol Biol. 2010 Jul 23;400(4):715-23. Epub 2010 May 24. PMID:20566411^[4]

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

References

↑ Candy L, Van Damme EJ, Peumans WJ, Menu-Bouaouiche L, Erard M, Rougé P. Structural and functional characterization of the GalNAc/Gal-specific lectin from the phytopathogenic ascomycete Sclerotinia sclerotiorum (Lib.) de Bary. Biochem Biophys Res Commun. 2003 Aug 22;308(2):396-402. PMID:12901882 doi:10.1016/s0006-291x(03)01406-2
↑ Van Damme EJ, Nakamura-Tsuruta S, Hirabayashi J, Rougé P, Peumans WJ. The Sclerotinia sclerotiorum agglutinin represents a novel family of fungal lectins remotely related to the Clostridium botulinum non-toxin haemagglutinin HA33/A. Glycoconj J. 2007 Apr;24(2-3):143-56. PMID:17294128 doi:10.1007/s10719-006-9022-z
↑ Sulzenbacher G, Roig-Zamboni V, Peumans WJ, Rouge P, Van Damme EJ, Bourne Y. Crystal structure of the GalNAc/Gal-specific agglutinin from the phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel adaptation of a beta-trefoil domain. J Mol Biol. 2010 Jul 23;400(4):715-23. Epub 2010 May 24. PMID:20566411 doi:10.1016/j.jmb.2010.05.038
↑ Sulzenbacher G, Roig-Zamboni V, Peumans WJ, Rouge P, Van Damme EJ, Bourne Y. Crystal structure of the GalNAc/Gal-specific agglutinin from the phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel adaptation of a beta-trefoil domain. J Mol Biol. 2010 Jul 23;400(4):715-23. Epub 2010 May 24. PMID:20566411 doi:10.1016/j.jmb.2010.05.038

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/2x2t"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2x2t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sclerotinia_sclerotiorum Sclerotinia sclerotiorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X2T FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</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]] 1.97&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2x2s|2x2s]]</div></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>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2x2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x2t OCA], [https://pdbe.org/2x2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x2t RCSB], [https://www.ebi.ac.uk/pdbsum/2x2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x2t ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/AGGL_SCLSC AGGL_SCLSC] Lectin that primarily recognizes glycans with a non-reducing terminal N-acetylgalactosamine (GalNAc), with a preference for the alpha- over the beta-anomer. Can also bind non-reducing terminal galactose (Gal) residues but with a lower affinity. Strongly interacts with glycolipid type glycans with terminal non-reducing Gal or GalNAc but fails to bind sialylated or fucosylated forms of the same glycans. Strongly interacts with galactosylated N-glycans, displaying highest affinity for alpha-1-3 branched mono-antennary N-glycans but also binding to multi-antennary glycans.<ref>PMID:12901882</ref> <ref>PMID:17294128</ref> <ref>PMID:20566411</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 38: @@
 [[Category: Large Structures]]
 [[Category: Sclerotinia sclerotiorum]]
-[[Category: Bourne, Y]]
+[[Category: Bourne Y]]
-[[Category: Damme, E J.M Van]]
+[[Category: Peumans WJ]]
-[[Category: Peumans, W J]]
+[[Category: Roig-Zamboni V]]
-[[Category: Roig-Zamboni, V]]
+[[Category: Rouge P]]
-[[Category: Rouge, P]]
+[[Category: Sulzenbacher G]]
-[[Category: Sulzenbacher, G]]
+[[Category: Van Damme EJM]]
-[[Category: Beta-trefoil domain]]
-[[Category: Cell adhesion]]
-[[Category: Fungal lectin]]

2x2t

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF SCLEROTINIA SCLEROTIORUM AGGLUTININ SSA in complex with Gal-beta1,3-Galnac

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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