6eke: Difference between revisions
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==crystal structure of a Pholiota squarrosa lectin unliganded== | |||
<StructureSection load='6eke' size='340' side='right' caption='[[6eke]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6eke]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EKE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EKE FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BU1:1,4-BUTANEDIOL'>BU1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6eke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eke OCA], [http://pdbe.org/6eke PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eke RCSB], [http://www.ebi.ac.uk/pdbsum/6eke PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eke ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We recombinantly produced and characterized the mini fungal lectin PhoSL. Despite a length of only 40 amino acids, PhoSL exclusively recognizes N-glycans with beta1,6-linked fucose. Core fucosylation influences the intrinsic properties and bioactivities of mammalian N-glycoproteins and its level is linked to various cancers. Thus, PhoSL serves as a promising tool for glycoprofiling. Without structural precedence, we solved its crystal structure using the zinc anomalous signal. We revealed an interlaced trimer creating a novel protein fold termed beta-prism III. Three biantennary core fucosylated N-glycan azides of 8 to 12 sugars were cocrystallized with PhoSL. The resulting highly resolved structures gave a detailed view on how the exclusive recognition of alpha1,6-fucosylated N-glycans by such a small protein occurs. This work also provided a protein consensus motif for the observed specificity as well as a glimpse on N-glycan flexibility upon binding. | |||
Recognition of complex core fucosylated N-glycans by a mini lectin.,Cabanettes A, Perkams L, Spies C, Unverzagt C, Varrot A Angew Chem Int Ed Engl. 2018 Jun 29. doi: 10.1002/anie.201805165. PMID:29956878<ref>PMID:29956878</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6eke" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cabanettes, A]] | [[Category: Cabanettes, A]] | ||
[[Category: Varrot, A]] | [[Category: Varrot, A]] | ||
[[Category: Lectin]] | |||
[[Category: Sugar binding protein]] | |||