2iho: Difference between revisions

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<StructureSection load='2iho' size='340' side='right'caption='[[2iho]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
<StructureSection load='2iho' size='340' side='right'caption='[[2iho]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2iho]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IHO FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.41&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iho OCA], [http://pdbe.org/2iho PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iho RCSB], [http://www.ebi.ac.uk/pdbsum/2iho PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iho ProSAT]</span></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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8X123_9AGAR Q8X123_9AGAR]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:17442345<ref>PMID:17442345</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2iho" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Agglutinin 3D structures|Agglutinin 3D structures]]
*[[Agglutinin 3D structures|Agglutinin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Marasmius oreades]]
[[Category: Marasmius oreades]]
[[Category: Askarieh, G]]
[[Category: Askarieh G]]
[[Category: Goldstein, I J]]
[[Category: Goldstein IJ]]
[[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, H C]]
[[Category: Winter HC]]
[[Category: Beta-trefoil]]
[[Category: Sugar binding protein]]

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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