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| | ==X-ray crystal structure of the Wbpe (WlbE) aminotransferase from pseudomonas aeruginosa as the PLP internal aldimine adduct with lysine 185== | | ==X-ray crystal structure of the Wbpe (WlbE) aminotransferase from pseudomonas aeruginosa as the PLP internal aldimine adduct with lysine 185== |
| - | <StructureSection load='3nyu' size='340' side='right' caption='[[3nyu]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='3nyu' size='340' side='right'caption='[[3nyu]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nyu]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NYU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nyu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NYU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.501Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nys|3nys]], [[3nyt|3nyt]]</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=3nyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nyu OCA], [https://pdbe.org/3nyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nyu RCSB], [https://www.ebi.ac.uk/pdbsum/3nyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nyu ProSAT]</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=3nyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nyu OCA], [http://pdbe.org/3nyu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nyu RCSB], [http://www.ebi.ac.uk/pdbsum/3nyu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nyu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/WBPE_PSEAE WBPE_PSEAE]] Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the amination of UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronic acid (UDP-3-oxo-D-GlcNAcA) to UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid (UDP-GlcNAc3NA), using L-glutamate as the preferred amine donor.<ref>PMID:18621892</ref> <ref>PMID:19282284</ref> <ref>PMID:19348502</ref> | + | [https://www.uniprot.org/uniprot/WBPE_PSEAE WBPE_PSEAE] Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the amination of UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronic acid (UDP-3-oxo-D-GlcNAcA) to UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid (UDP-GlcNAc3NA), using L-glutamate as the preferred amine donor.<ref>PMID:18621892</ref> <ref>PMID:19282284</ref> <ref>PMID:19348502</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ny/3nyu_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ny/3nyu_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | ==See Also== | | ==See Also== |
| - | *[[Aminotransferase|Aminotransferase]] | + | *[[Aminotransferase 3D structures|Aminotransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Holden, H M]] | + | [[Category: Large Structures]] |
| - | [[Category: Thoden, J B]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Aminotransferase]] | + | [[Category: Holden HM]] |
| - | [[Category: Nucleotide-sugar binding]] | + | [[Category: Thoden JB]] |
| - | [[Category: Plp binding]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
WBPE_PSEAE Plays a role in the biosynthesis of B-band O antigen for serotype O5. Catalyzes the amination of UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronic acid (UDP-3-oxo-D-GlcNAcA) to UDP-2-acetamido-3-amino-2,3-dideoxy-D-glucuronic acid (UDP-GlcNAc3NA), using L-glutamate as the preferred amine donor.[1] [2] [3]
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
Campylobacter jejuni is a Gram-negative bacterium that represents a leading cause of human gastroenteritis worldwide. Of particular concern is the link between C. jejuni infections and the subsequent development of Guillain-Barre syndrome, an acquired autoimmune disorder leading to paralysis. All Gram-negative bacteria contain complex glycoconjugates anchored to their outer membranes, but in most strains of C. jejuni, this lipoglycan lacks the O-antigen repeating units. Recent mass spectrometry analyses indicate that the C. jejuni 81116 (Penner serotype HS:6) lipoglycan contains two dideoxyhexosamine residues, and enzymological assay data show that this bacterial strain can synthesize both dTDP-3-acetamido-3,6-dideoxy-d-glucose and dTDP-3-acetamido-3,6-dideoxy-d-galactose. The focus of this investigation is on WlaRG from C. jejuni, which plays a key role in the production of these unusual sugars by functioning as a pyridoxal 5'-phosphate dependent aminotransferase. Here we describe the first three-dimensional structures of the enzyme in various complexes determined to resolutions of 1.7 A or higher. Of particular significance are the external aldimine structures of WlaRG solved in the presence of either dTDP-3-amino-3,6-dideoxy-d-galactose or dTDP-3-amino-3,6-dideoxy-d-glucose. These models highlight the manner in which WlaRG can accommodate sugars with differing stereochemistries about their C-4' carbon positions. In addition, we present a corrected structure of WbpE, a related sugar aminotransferase from Pseudomonas aeruginosa, solved to 1.3 A resolution. This article is protected by copyright. All rights reserved.
Structural Investigation on WlaRG from Campylobacter jejuni: A Sugar Aminotransferase.,Dow GT, Gilbert M, Thoden JB, Holden HM Protein Sci. 2016 Dec 28. doi: 10.1002/pro.3109. PMID:28028852[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Westman EL, Preston A, Field RA, Lam JS. Biosynthesis of a rare di-N-acetylated sugar in the lipopolysaccharides of both Pseudomonas aeruginosa and Bordetella pertussis occurs via an identical scheme despite different gene clusters. J Bacteriol. 2008 Sep;190(18):6060-9. doi: 10.1128/JB.00579-08. Epub 2008 Jul 11. PMID:18621892 doi:10.1128/JB.00579-08
- ↑ Westman EL, McNally DJ, Charchoglyan A, Brewer D, Field RA, Lam JS. Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa. J Biol Chem. 2009 May 1;284(18):11854-62. doi: 10.1074/jbc.M808583200. Epub 2009 , Mar 12. PMID:19282284 doi:10.1074/jbc.M808583200
- ↑ Larkin A, Imperiali B. Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1. Biochemistry. 2009 Jun 16;48(23):5446-55. doi: 10.1021/bi900186u. PMID:19348502 doi:10.1021/bi900186u
- ↑ Dow GT, Gilbert M, Thoden JB, Holden HM. Structural Investigation on WlaRG from Campylobacter jejuni: A Sugar Aminotransferase. Protein Sci. 2016 Dec 28. doi: 10.1002/pro.3109. PMID:28028852 doi:http://dx.doi.org/10.1002/pro.3109
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