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[[Image:2iho.jpg|left|200px]]<br /><applet load="2iho" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2iho, resolution 2.41&Aring;" />
'''Crystal structure of MOA, a lectin from the mushroom Marasmius oreades in complex with the trisaccharide Gal(1,3)Gal(1,4)GlcNAc'''<br />


==Overview==
==Crystal structure of MOA, a lectin from the mushroom Marasmius oreades in complex with the trisaccharide Gal(1,3)Gal(1,4)GlcNAc==
MOA, a lectin from the mushroom Marasmius oreades, is one of the few reagents that specifically agglutinate blood group B erythrocytes. Further, it is the only lectin known to have exclusive specificity for Galalpha(1,3)Gal-containing sugar epitopes, which are antigens that pose a severe barrier to animal-to-human organ transplantation. We describe here the structure of MOA at 2.4 A resolution, in complex with the linear trisaccharide Galalpha(1,3)Galbeta(1,4)GlcNAc. The structure is dimeric, with two distinct domains per protomer: the N-terminal lectin module adopts a ricinB/beta-trefoil fold and contains three putative carbohydrate-binding sites, while the C-terminal domain serves as a dimerization interface. This latter domain, which has an unknown function, reveals a novel fold with intriguing conservation of an active site cleft. A number of indications suggest that MOA may have an enzymatic function in addition to the sugar-binding properties.
<StructureSection load='2iho' size='340' side='right'caption='[[2iho]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2iho]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Marasmius_oreades Marasmius oreades]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IHO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.41&#8491;</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=2iho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iho OCA], [https://pdbe.org/2iho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iho RCSB], [https://www.ebi.ac.uk/pdbsum/2iho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iho ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8X123_9AGAR Q8X123_9AGAR]
== 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/ih/2iho_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=2iho ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2IHO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Marasmius_oreades Marasmius oreades]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IHO OCA].
*[[Agglutinin 3D structures|Agglutinin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of the Marasmius oreades mushroom lectin in complex with a xenotransplantation epitope., Grahn E, Askarieh G, Holmner A, Tateno H, Winter HC, Goldstein IJ, Krengel U, J Mol Biol. 2007 Jun 8;369(3):710-21. Epub 2007 Mar 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17442345 17442345]
[[Category: Large Structures]]
[[Category: Marasmius oreades]]
[[Category: Marasmius oreades]]
[[Category: Single protein]]
[[Category: Askarieh G]]
[[Category: Askarieh, G.]]
[[Category: Goldstein IJ]]
[[Category: Goldstein, I J.]]
[[Category: Grahn E]]
[[Category: Grahn, E.]]
[[Category: Holmner A]]
[[Category: Holmner, A.]]
[[Category: Krengel U]]
[[Category: Krengel, U.]]
[[Category: Tateno H]]
[[Category: Tateno, H.]]
[[Category: Winter HC]]
[[Category: Winter, H C.]]
[[Category: beta-trefoil]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:47 2008''

Latest revision as of 12:03, 21 February 2024

Crystal structure of MOA, a lectin from the mushroom Marasmius oreades in complex with the trisaccharide Gal(1,3)Gal(1,4)GlcNAcCrystal structure of MOA, a lectin from the mushroom Marasmius oreades in complex with the trisaccharide Gal(1,3)Gal(1,4)GlcNAc

Structural highlights

2iho is a 1 chain structure with sequence from Marasmius oreades. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.41Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8X123_9AGAR

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2iho, resolution 2.41Å

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