2fmd: Difference between revisions
Jump to navigation
Jump to search
m Protected "2fmd" [edit=sysop:move=sysop] |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Structural basis of carbohydrate recognition by Bowringia milbraedii seed agglutinin== | |||
<StructureSection load='2fmd' size='340' side='right'caption='[[2fmd]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2fmd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leucomphalos_mildbraedii Leucomphalos mildbraedii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FMD 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]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASX:ASP/ASN+AMBIGUOUS'>ASX</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PRD_900111:2alpha-alpha-mannobiose'>PRD_900111</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=2fmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmd OCA], [https://pdbe.org/2fmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fmd RCSB], [https://www.ebi.ac.uk/pdbsum/2fmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fmd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LEC_LEUMI LEC_LEUMI] Binds preferentially to oligosaccharides bearing the sequence Man-alpha-1->2 Man-alpha-1->6 Man-alpha-1->6Man found in early steps of glycoprotein processing in the endoplasmic reticulum. It binds weakly to highly processed oligosaccharide structures.<ref>PMID:2925660</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/fm/2fmd_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=2fmd ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of the seed lectin from the tropical legume Bowringia milbraedii was determined in complex with the disaccharide ligand Man(alpha1-2)Man. In solution, the protein exhibits a dynamic dimer-tetramer equilibrium, consistent with the concanavalin A-type tetramer observed in the crystal. Contacts between the tetramers are mediated almost exclusively through the carbohydrate ligand, resulting in a crystal lattice virtually identical to that of the concanavalin-A:Man(alpha1-2)Man complex, even though both proteins have less than 50% sequence identity. The disaccharide binds exclusively in a "downstream" binding mode, with the non-reducing mannose occupying the monosaccharide-binding site. The reducing mannose is bound in a predominantly polar subsite involving Tyr131, Gln218, and Tyr219. | |||
Structural basis of carbohydrate recognition by a Man(alpha1-2)Man-specific lectin from Bowringia milbraedii.,Buts L, Garcia-Pino A, Wyns L, Loris R Glycobiology. 2006 Jul;16(7):635-40. Epub 2006 Mar 27. PMID:16567368<ref>PMID:16567368</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2fmd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Leucomphalos mildbraedii]] | [[Category: Leucomphalos mildbraedii]] | ||
[[Category: Buts | [[Category: Buts L]] | ||
[[Category: Garcia-Pino | [[Category: Garcia-Pino A]] | ||
[[Category: Loris | [[Category: Loris R]] | ||
[[Category: Wyns | [[Category: Wyns L]] | ||
Latest revision as of 12:29, 30 August 2023
Structural basis of carbohydrate recognition by Bowringia milbraedii seed agglutininStructural basis of carbohydrate recognition by Bowringia milbraedii seed agglutinin
Structural highlights
FunctionLEC_LEUMI Binds preferentially to oligosaccharides bearing the sequence Man-alpha-1->2 Man-alpha-1->6 Man-alpha-1->6Man found in early steps of glycoprotein processing in the endoplasmic reticulum. It binds weakly to highly processed oligosaccharide structures.[1] 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 PubMedThe crystal structure of the seed lectin from the tropical legume Bowringia milbraedii was determined in complex with the disaccharide ligand Man(alpha1-2)Man. In solution, the protein exhibits a dynamic dimer-tetramer equilibrium, consistent with the concanavalin A-type tetramer observed in the crystal. Contacts between the tetramers are mediated almost exclusively through the carbohydrate ligand, resulting in a crystal lattice virtually identical to that of the concanavalin-A:Man(alpha1-2)Man complex, even though both proteins have less than 50% sequence identity. The disaccharide binds exclusively in a "downstream" binding mode, with the non-reducing mannose occupying the monosaccharide-binding site. The reducing mannose is bound in a predominantly polar subsite involving Tyr131, Gln218, and Tyr219. Structural basis of carbohydrate recognition by a Man(alpha1-2)Man-specific lectin from Bowringia milbraedii.,Buts L, Garcia-Pino A, Wyns L, Loris R Glycobiology. 2006 Jul;16(7):635-40. Epub 2006 Mar 27. PMID:16567368[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||