2x2t: Difference between revisions

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[[Image:2x2t.png|left|200px]]


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==CRYSTAL STRUCTURE OF SCLEROTINIA SCLEROTIORUM AGGLUTININ SSA in complex with Gal-beta1,3-Galnac==
The line below this paragraph, containing "STRUCTURE_2x2t", creates the "Structure Box" on the page.
<StructureSection load='2x2t' size='340' side='right'caption='[[2x2t]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
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<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>
{{STRUCTURE_2x2t|  PDB=2x2t  |  SCENE=  }}
<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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x2/2x2t_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2x2t ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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 SCLEROTINIA SCLEROTIORUM AGGLUTININ SSA IN COMPLEX WITH GAL-BETA1,3-GALNAC===
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<ref>PMID:20566411</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2x2t" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_20566411}}, adds the Publication Abstract to the page
*[[Agglutinin 3D structures|Agglutinin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 20566411 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_20566411}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2X2T is a 1 chain structure with sequence from [http://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].
 
==Reference==
<ref group="xtra">PMID:20566411</ref><references group="xtra"/>
[[Category: Sclerotinia sclerotiorum]]
[[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]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  7 08:18:12 2010''

Latest revision as of 13:22, 20 December 2023

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

See Also

References

  1. ↑ 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
  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
  3. ↑ 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
  4. ↑ 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

2x2t, resolution 1.97Å

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