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==Molecular structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen== | |||
<StructureSection load='4ayl' size='340' side='right' caption='[[4ayl]], [[Resolution|resolution]] 1.92Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ayl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacteroides_fragilis_subsp._ovatus"_(eggerth_and_gagnon_1933)_holdeman_and_moore_1970 "bacteroides fragilis subsp. ovatus" (eggerth and gagnon 1933) holdeman and moore 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AYL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AYL FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ayj|4ayj]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycoprotein-fucosylgalactoside_alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.40 2.4.1.40] </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=4ayl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ayl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ayl RCSB], [http://www.ebi.ac.uk/pdbsum/4ayl PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Glycosyltransferase|Glycosyltransferase]] | *[[Glycosyltransferase|Glycosyltransferase]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase]] | [[Category: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase]] | ||
[[Category: Acharya, K R | [[Category: Acharya, K R]] | ||
[[Category: Brewb, K | [[Category: Brewb, K]] | ||
[[Category: Lizotte-Waniewskib, M | [[Category: Lizotte-Waniewskib, M]] | ||
[[Category: Pham, T T.K | [[Category: Pham, T T.K]] | ||
[[Category: Stinsonb, B | [[Category: Stinsonb, B]] | ||
[[Category: Sundriyala, A | [[Category: Sundriyala, A]] | ||
[[Category: Thiyagarajan, N | [[Category: Thiyagarajan, N]] | ||
[[Category: Tumbale, P | [[Category: Tumbale, P]] | ||
[[Category: Histo-blood group enzyme]] | [[Category: Histo-blood group enzyme]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 20:39, 21 December 2014
Molecular structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigenMolecular structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen
Structural highlights
Publication Abstract from PubMedHisto-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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