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[[Image:3ues.png|left|200px]]
==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]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ues]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum_subsp._infantis_atcc_15697_=_jcm_1222 Bifidobacterium longum subsp. infantis atcc 15697 = jcm 1222]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UES FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mo4|3mo4]], [[3uet|3uet]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLIJ_2413, Blon_2336 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=391904 Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1,3-alpha-L-fucosidase 1,3-alpha-L-fucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.111 3.2.1.111] </span></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=3ues FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ues OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ues RCSB], [http://www.ebi.ac.uk/pdbsum/3ues PDBsum]</span></td></tr>
</table>
<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.


{{STRUCTURE_3ues|  PDB=3ues  |  SCENE=  }}
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>


===Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_22451675}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[3ues]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_longum_subsp._infantis_atcc_15697_=_jcm_1222 Bifidobacterium longum subsp. infantis atcc 15697 = jcm 1222]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UES OCA].
</StructureSection>
[[Category: 1,3-alpha-L-fucosidase]]
[[Category: 1,3-alpha-L-fucosidase]]
[[Category: Bifidobacterium longum subsp. infantis atcc 15697 = jcm 1222]]
[[Category: Bifidobacterium longum subsp. infantis atcc 15697 = jcm 1222]]
[[Category: Ashida, H.]]
[[Category: Ashida, H]]
[[Category: Fushinobu, S.]]
[[Category: Fushinobu, S]]
[[Category: Hidaka, M.]]
[[Category: Hidaka, M]]
[[Category: Honda, Y.]]
[[Category: Honda, Y]]
[[Category: Katayama, T.]]
[[Category: Katayama, T]]
[[Category: Kitaoka, M.]]
[[Category: Kitaoka, M]]
[[Category: Kumagai, H.]]
[[Category: Kumagai, H]]
[[Category: Sakurama, H.]]
[[Category: Sakurama, H]]
[[Category: Yamamoto, K.]]
[[Category: Yamamoto, K]]
[[Category: Yoshida, E.]]
[[Category: Yoshida, E]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]