4ayl: Difference between revisions
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==Molecular structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen== | ==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=''> | <StructureSection load='4ayl' size='340' side='right'caption='[[4ayl]], [[Resolution|resolution]] 1.92Å' scene=''> | ||
== Structural highlights == | == 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> | <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> | ||
Revision as of 12:44, 6 March 2019
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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