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1iub
From Proteopedia
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| - | [[Image:1iub.jpg|left|200px]] | ||
| - | + | ==Fucose-specific lectin from Aleuria aurantia (Hg-derivative form)== | |
| - | + | <StructureSection load='1iub' size='340' side='right'caption='[[1iub]], [[Resolution|resolution]] 2.31Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[1iub]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aleuria_aurantia Aleuria aurantia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IUB 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]] 2.31Å</td></tr> | |
| - | | | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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=1iub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iub OCA], [https://pdbe.org/1iub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iub RCSB], [https://www.ebi.ac.uk/pdbsum/1iub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iub ProSAT], [https://www.topsan.org/Proteins/RSGI/1iub TOPSAN]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/LECF_ALEAU LECF_ALEAU] Might have a role in the differentiation of cells. Binds L-fucose. | |
| - | + | == 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/iu/1iub_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=1iub ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Aleuria aurantia possesses a fucose-specific lectin (AAL) that is widely used as a specific probe for fucose. Fucosylated sugars often play pivotal roles in many cellular processes. We have determined the crystal structure of AAL at 2.24 A resolution in complex with only three fucose molecules in its five sugar binding sites of a six-fold beta-propeller structure. Very recently, the structure of AAL has been independently determined, showing that all the five binding sites were occupied by fucose molecules [Wimmerova, M., et al. (2003) J. Biol. Chem. 278, 27059-27067]. Stabilization of the arginine conformation bound to fucose molecules plays an essential role in generating the difference in the affinity in the five binding sites. Binding models with a couple of saccharides based on biochemical assays suggest that hydrophobic contacts also play important roles in AAL recognizing its ligand. | Aleuria aurantia possesses a fucose-specific lectin (AAL) that is widely used as a specific probe for fucose. Fucosylated sugars often play pivotal roles in many cellular processes. We have determined the crystal structure of AAL at 2.24 A resolution in complex with only three fucose molecules in its five sugar binding sites of a six-fold beta-propeller structure. Very recently, the structure of AAL has been independently determined, showing that all the five binding sites were occupied by fucose molecules [Wimmerova, M., et al. (2003) J. Biol. Chem. 278, 27059-27067]. Stabilization of the arginine conformation bound to fucose molecules plays an essential role in generating the difference in the affinity in the five binding sites. Binding models with a couple of saccharides based on biochemical assays suggest that hydrophobic contacts also play important roles in AAL recognizing its ligand. | ||
| - | + | Crystal structure of fucose-specific lectin from Aleuria aurantia binding ligands at three of its five sugar recognition sites.,Fujihashi M, Peapus DH, Kamiya N, Nagata Y, Miki K Biochemistry. 2003 Sep 30;42(38):11093-9. PMID:14503859<ref>PMID:14503859</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1iub" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Aleuria aurantia]] | [[Category: Aleuria aurantia]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Fujihashi | + | [[Category: Fujihashi M]] |
| - | [[Category: Kamiya | + | [[Category: Kamiya N]] |
| - | [[Category: Miki | + | [[Category: Miki K]] |
| - | [[Category: Nagata | + | [[Category: Nagata Y]] |
| - | [[Category: Peapus | + | [[Category: Peapus DH]] |
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Current revision
Fucose-specific lectin from Aleuria aurantia (Hg-derivative form)
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