4x6l
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4x6l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_21178 Staphylococcus aureus subsp. aureus 21178]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X6L FirstGlance]. <br> | <table><tr><td colspan='2'>[[4x6l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_21178 Staphylococcus aureus subsp. aureus 21178]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X6L FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.19Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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=4x6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x6l OCA], [https://pdbe.org/4x6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x6l RCSB], [https://www.ebi.ac.uk/pdbsum/4x6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x6l ProSAT]</span></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=4x6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x6l OCA], [https://pdbe.org/4x6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x6l RCSB], [https://www.ebi.ac.uk/pdbsum/4x6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x6l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TARM_STAAC TARM_STAAC] Attaches N-acetyl-alpha-D-glucosamine residues to poly(RboP)-wall teichoic acids (WTAs).<ref>PMID:20185825</ref> <ref>PMID:25624472</ref> <ref>PMID:25697358</ref> | [https://www.uniprot.org/uniprot/TARM_STAAC TARM_STAAC] Attaches N-acetyl-alpha-D-glucosamine residues to poly(RboP)-wall teichoic acids (WTAs).<ref>PMID:20185825</ref> <ref>PMID:25624472</ref> <ref>PMID:25697358</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Unique to Gram-positive bacteria, wall teichoic acids are anionic glycopolymers cross-stitched to a thick layer of peptidoglycan. The polyol phosphate subunits of these glycopolymers are decorated with GlcNAc sugars that are involved in phage binding, genetic exchange, host antibody response, resistance, and virulence. The search for the enzymes responsible for GlcNAcylation in Staphylococcus aureus has recently identified TarM and TarS with respective alpha- and beta-(1-4) glycosyltransferase activities. The stereochemistry of the GlcNAc attachment is important in balancing biological processes, such that the interplay of TarM and TarS is likely important for bacterial pathogenicity and survival. Here we present the crystal structure of TarM in an unusual ternary-like complex consisting of a polymeric acceptor substrate analog, UDP from a hydrolyzed donor, and an alpha-glyceryl-GlcNAc product formed in situ. These structures support an internal nucleophilic substitution-like mechanism, lend new mechanistic insight into the glycosylation of glycopolymers, and reveal a trimerization domain with a likely role in acceptor substrate scaffolding. | ||
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| - | Structure and mechanism of Staphylococcus aureus TarM, the wall teichoic acid alpha-glycosyltransferase.,Sobhanifar S, Worrall LJ, Gruninger RJ, Wasney GA, Blaukopf M, Baumann L, Lameignere E, Solomonson M, Brown ED, Withers SG, Strynadka NC Proc Natl Acad Sci U S A. 2015 Feb 10;112(6):E576-85. doi:, 10.1073/pnas.1418084112. Epub 2015 Jan 26. PMID:25624472<ref>PMID:25624472</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4x6l" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of S. aureus TarM in complex with UDP
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