View source for 4ayj


==Molecular structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen==
<StructureSection load='4ayj' size='340' side='right'caption='[[4ayj]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ayj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_ovatus Bacteroides ovatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AYJ 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900070:2-fucosyllactose'>PRD_900070</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=4ayj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ayj OCA], [https://pdbe.org/4ayj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ayj RCSB], [https://www.ebi.ac.uk/pdbsum/4ayj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ayj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A7LVT2_BACO1 A7LVT2_BACO1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Histo-blood group antigens (HBGAs) are a source of antigenic variation between individuals that modulates resistance and susceptibility to pathogens and is a barrier to the spread of enveloped viruses. HBGAs are also produced by a few prokaryotes where they are synthesized by glycosyltransferases (GTs) related to human HBGA synthases. Here we report the first structure of a bacterial GT of this family, from an intestinal resident, Bacteroides ovatus. Unlike its mammalian homologues and other GTs with similar folds, this protein lacks a metal-binding Asp-X-Asp motif and is fully active in the absence of divalent metal ions, yet is strikingly similar in structure and in its interactions with substrates to structurally characterized mammalian metal-dependent mammalian homologues. This shows how an apparently major divergence in catalytic properties can be accommodated by minor structural adjustments and illustrates the structural underpinnings of horizontal transfer of a functional gene from prokaryotes to vertebrates.

Structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen.,Thiyagarajan N, Pham TT, Stinson B, Sundriyal A, Tumbale P, Lizotte-Waniewski M, Brew K, Acharya KR Sci Rep. 2012;2:940. doi: 10.1038/srep00940. Epub 2012 Dec 7. PMID:23230506<ref>PMID:23230506</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ayj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacteroides ovatus]]
[[Category: Large Structures]]
[[Category: Acharya KR]]
[[Category: Brewb K]]
[[Category: Lizotte-Waniewskib M]]
[[Category: Pham TTK]]
[[Category: Stinson B]]
[[Category: Sundriyal A]]
[[Category: Thiyagarajan N]]
[[Category: Tumbale P]]