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| | <StructureSection load='2ft0' size='340' side='right'caption='[[2ft0]], [[Resolution|resolution]] 1.66Å' scene=''> | | <StructureSection load='2ft0' size='340' side='right'caption='[[2ft0]], [[Resolution|resolution]] 1.66Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ft0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecol6 Ecol6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FT0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ft0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_CFT073 Escherichia coli CFT073]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FT0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</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]] 1.66Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fs5|2fs5]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">wecd ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=199310 ECOL6])</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=2ft0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ft0 OCA], [https://pdbe.org/2ft0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ft0 RCSB], [https://www.ebi.ac.uk/pdbsum/2ft0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ft0 ProSAT], [https://www.topsan.org/Proteins/BSGI/2ft0 TOPSAN]</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=2ft0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ft0 OCA], [https://pdbe.org/2ft0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ft0 RCSB], [https://www.ebi.ac.uk/pdbsum/2ft0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ft0 ProSAT], [https://www.topsan.org/Proteins/BSGI/2ft0 TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/WECD_ECOL6 WECD_ECOL6]] Catalyzes the acetylation of dTDP-fucosamine (dTDP-4-amino-4,6-dideoxy-D-galactose) to dTDP-Fuc4NAc, which is utilized in the biosynthesis of the enterobacterial common antigen (ECA).[HAMAP-Rule:MF_02027]<ref>PMID:16855251</ref>
| + | [https://www.uniprot.org/uniprot/WECD_ECOL6 WECD_ECOL6] Catalyzes the acetylation of dTDP-fucosamine (dTDP-4-amino-4,6-dideoxy-D-galactose) to dTDP-Fuc4NAc, which is utilized in the biosynthesis of the enterobacterial common antigen (ECA).[HAMAP-Rule:MF_02027]<ref>PMID:16855251</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecol6]] | + | [[Category: Escherichia coli CFT073]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Hung MN]] |
| - | [[Category: Hung, M N]] | + | [[Category: Matte A]] |
| - | [[Category: Matte, A]] | + | [[Category: Munger C]] |
| - | [[Category: Munger, C]] | + | [[Category: Nadeau G]] |
| - | [[Category: Nadeau, G]] | + | [[Category: Rangarajan E]] |
| - | [[Category: Rangarajan, E]] | + | [[Category: Sulea T]] |
| - | [[Category: Sulea, T]] | + | |
| - | [[Category: Bsgi]]
| + | |
| - | [[Category: Gnat fold acetyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
WECD_ECOL6 Catalyzes the acetylation of dTDP-fucosamine (dTDP-4-amino-4,6-dideoxy-D-galactose) to dTDP-Fuc4NAc, which is utilized in the biosynthesis of the enterobacterial common antigen (ECA).[HAMAP-Rule:MF_02027][1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Enterobacterial common antigen (ECA) is a polysaccharide found on the outer membrane of virtually all gram-negative enteric bacteria and consists of three sugars, N-acetyl-d-glucosamine, N-acetyl-d-mannosaminuronic acid, and 4-acetamido-4,6-dideoxy-d-galactose, organized into trisaccharide repeating units having the sequence -->3)-alpha-d-Fuc4NAc-(1-->4)-beta-d-ManNAcA-(1-->4)-alpha-d-GlcNAc-(1-->. While the precise function of ECA is unknown, it has been linked to the resistance of Shiga-toxin-producing Escherichia coli (STEC) O157:H7 to organic acids and the resistance of Salmonella enterica to bile salts. The final step in the synthesis of 4-acetamido-4,6-dideoxy-d-galactose, the acetyl-coenzyme A (CoA)-dependent acetylation of the 4-amino group, is carried out by TDP-fucosamine acetyltransferase (WecD). We have determined the crystal structure of WecD in apo form at a 1.95-Angstrom resolution and bound to acetyl-CoA at a 1.66-Angstrom resolution. WecD is a dimeric enzyme, with each monomer adopting the GNAT N-acetyltransferase fold, common to a number of enzymes involved in acetylation of histones, aminoglycoside antibiotics, serotonin, and sugars. The crystal structure of WecD, however, represents the first structure of a GNAT family member that acts on nucleotide sugars. Based on this cocrystal structure, we have used flexible docking to generate a WecD-bound model of the acetyl-CoA-TDP-fucosamine tetrahedral intermediate, representing the structure during acetyl transfer. Our structural data show that WecD does not possess a residue that directly functions as a catalytic base, although Tyr208 is well positioned to function as a general acid by protonating the thiolate anion of coenzyme A.
Crystal structure of TDP-fucosamine acetyltransferase (WecD) from Escherichia coli, an enzyme required for enterobacterial common antigen synthesis.,Hung MN, Rangarajan E, Munger C, Nadeau G, Sulea T, Matte A J Bacteriol. 2006 Aug;188(15):5606-17. PMID:16855251[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hung MN, Rangarajan E, Munger C, Nadeau G, Sulea T, Matte A. Crystal structure of TDP-fucosamine acetyltransferase (WecD) from Escherichia coli, an enzyme required for enterobacterial common antigen synthesis. J Bacteriol. 2006 Aug;188(15):5606-17. PMID:16855251 doi:http://dx.doi.org/188/15/5606
- ↑ Hung MN, Rangarajan E, Munger C, Nadeau G, Sulea T, Matte A. Crystal structure of TDP-fucosamine acetyltransferase (WecD) from Escherichia coli, an enzyme required for enterobacterial common antigen synthesis. J Bacteriol. 2006 Aug;188(15):5606-17. PMID:16855251 doi:http://dx.doi.org/188/15/5606
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