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| | <StructureSection load='5wfg' size='340' side='right'caption='[[5wfg]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='5wfg' size='340' side='right'caption='[[5wfg]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wfg]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Theia Theia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WFG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WFG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wfg]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoanaerobacter_italicus_Ab9 Thermoanaerobacter italicus Ab9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WFG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Thit_1850 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=580331 THEIA])</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=5wfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wfg OCA], [https://pdbe.org/5wfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wfg RCSB], [https://www.ebi.ac.uk/pdbsum/5wfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wfg ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylglucosaminyldiphosphoundecaprenol_N-acetyl-beta-D-_mannosaminyltransferase N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D- mannosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.187 2.4.1.187] </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=5wfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wfg OCA], [http://pdbe.org/5wfg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wfg RCSB], [http://www.ebi.ac.uk/pdbsum/5wfg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wfg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/D3T4E0_THEIA D3T4E0_THEIA]] Catalyzes the conversion of GlcNAc-PP-undecaprenol into ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate in the de novo synthesis of teichoic acid.[HAMAP-Rule:MF_02070] | + | [https://www.uniprot.org/uniprot/D3T4E0_THEIA D3T4E0_THEIA] Catalyzes the conversion of GlcNAc-PP-undecaprenol into ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate in the de novo synthesis of teichoic acid.[HAMAP-Rule:MF_02070] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D- mannosaminyltransferase]] | + | [[Category: Thermoanaerobacter italicus Ab9]] |
| - | [[Category: Theia]]
| + | [[Category: Cascio D]] |
| - | [[Category: Cascio, D]] | + | [[Category: Clubb RT]] |
| - | [[Category: Clubb, R T]] | + | [[Category: Kattke MD]] |
| - | [[Category: Kattke, M D]] | + | [[Category: Sawaya MR]] |
| - | [[Category: Sawaya, M R]] | + | |
| - | [[Category: Beta-n-acetylmannosaminyltransferase]]
| + | |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Wall teichoic acid enzyme]]
| + | |
| Structural highlights
Function
D3T4E0_THEIA Catalyzes the conversion of GlcNAc-PP-undecaprenol into ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate in the de novo synthesis of teichoic acid.[HAMAP-Rule:MF_02070]
Publication Abstract from PubMed
Staphylococcus aureus and other bacterial pathogens affix wall teichoic acids (WTAs) to their surface. These highly abundant anionic glycopolymers have critical functions in bacterial physiology and their susceptibility to beta-lactam antibiotics. The membrane-associated TagA glycosyltransferase (GT) catalyzes the first-committed step in WTA biosynthesis and is a founding member of the WecB/TagA/CpsF GT family, more than 6,000 enzymes that synthesize a range of extracellular polysaccharides through a poorly understood mechanism. Crystal structures of TagA from T. italicus in its apo- and UDP-bound states reveal a novel GT fold, and coupled with biochemical and cellular data define the mechanism of catalysis. We propose that enzyme activity is regulated by interactions with the bilayer, which trigger a structural change that facilitates proper active site formation and recognition of the enzyme's lipid-linked substrate. These findings inform upon the molecular basis of WecB/TagA/CpsF activity and could guide the development of new anti-microbial drugs.
Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria.,Kattke MD, Gosschalk JE, Martinez OE, Kumar G, Gale RT, Cascio D, Sawaya MR, Philips M, Brown ED, Clubb RT PLoS Pathog. 2019 Apr 19;15(4):e1007723. doi: 10.1371/journal.ppat.1007723., eCollection 2019 Apr. PMID:31002736[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kattke MD, Gosschalk JE, Martinez OE, Kumar G, Gale RT, Cascio D, Sawaya MR, Philips M, Brown ED, Clubb RT. Structure and mechanism of TagA, a novel membrane-associated glycosyltransferase that produces wall teichoic acids in pathogenic bacteria. PLoS Pathog. 2019 Apr 19;15(4):e1007723. doi: 10.1371/journal.ppat.1007723., eCollection 2019 Apr. PMID:31002736 doi:http://dx.doi.org/10.1371/journal.ppat.1007723
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