3ues: Difference between revisions
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< | ==Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin== | ||
<StructureSection load='3ues' size='340' side='right'caption='[[3ues]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ues]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum_subsp._infantis_ATCC_15697_=_JCM_1222_=_DSM_20088 Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UES 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]] 1.6Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DFU:(2S,3R,4S,5R)-2-METHYLPIPERIDINE-3,4,5-TRIOL'>DFU</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=3ues FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ues OCA], [https://pdbe.org/3ues PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ues RCSB], [https://www.ebi.ac.uk/pdbsum/3ues PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ues ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B7GNN8_BIFLS B7GNN8_BIFLS] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
alpha-L-fucosyl residues attached at the non-reducing ends of glycoconjugates constitute histo-blood group antigens Lewis (Le) and ABO and play fundamental roles in various biological processes. Therefore, establishing a method for synthesizing the antigens is important for functional glycomics studies. However, regiospecific synthesis of glycosyl linkages, especially alpha-L-fucosyl linkages, is quite difficult to control both by chemists and enzymologists. Here, we generated an alpha-L-fucosynthase that specifically introduces Le(a) and Le(x) antigens into the type-1 and type-2 chains, respectively; i.e. the enzyme specifically accepts the disaccharide structures (Galbeta1-3/4GlcNAc) at the non-reducing ends and attaches a Fuc residue via an alpha-(1,4/3)-linkage to the GlcNAc. X-ray crystallographic studies revealed the structural basis of this strict regio- and acceptor specificity, which includes the induced fit movement of the catalytically important residues, and the difference between the active site structures of 1,3-1,4-alpha-L-fucosidase (EC 3.2.1.111) and alpha-L-fucosidase (EC 3.2.1.51) in glycoside hydrolase family 29. The glycosynthase developed in this study should serve as a potentially powerful tool to specifically introduce the Le(a/x) epitopes onto labile glycoconjugates including glycoproteins. Mining glycosidases with strict specificity may represent the most efficient route to the specific synthesis of glycosidic bonds. | |||
1,3-1,4-alpha-L-fucosynthase that specifically introduces Lewis a/x antigens into type-1/2 chains.,Sakurama H, Fushinobu S, Hidaka M, Yoshida E, Honda Y, Ashida H, Kitaoka M, Kumagai H, Yamamoto K, Katayama T J Biol Chem. 2012 May 11;287(20):16709-19. Epub 2012 Mar 26. PMID:22451675<ref>PMID:22451675</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
[[ | <div class="pdbe-citations 3ues" style="background-color:#fffaf0;"></div> | ||
== References == | |||
[[Category: | <references/> | ||
[[Category: Ashida | __TOC__ | ||
[[Category: Fushinobu | </StructureSection> | ||
[[Category: Hidaka | [[Category: Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]] | ||
[[Category: Honda | [[Category: Large Structures]] | ||
[[Category: Katayama | [[Category: Ashida H]] | ||
[[Category: Kitaoka | [[Category: Fushinobu S]] | ||
[[Category: Kumagai | [[Category: Hidaka M]] | ||
[[Category: Sakurama | [[Category: Honda Y]] | ||
[[Category: Yamamoto | [[Category: Katayama T]] | ||
[[Category: Yoshida | [[Category: Kitaoka M]] | ||
[[Category: Kumagai H]] | |||
[[Category: Sakurama H]] | |||
[[Category: Yamamoto K]] | |||
[[Category: Yoshida E]] | |||
Latest revision as of 17:35, 1 November 2023
Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin
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