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3nys

From Proteopedia

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X-ray structure of the K185A mutant of WbpE (WlbE) from pseudomonas aeruginosa in complex with PLP at 1.45 angstrom resolution

Structural highlights

3nys is a 1 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.45Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3nys"

Categories: Large Structures | Pseudomonas aeruginosa PAO1 | Holden HM | Thoden JB

@@ Line 1: / Line 1: @@
 ==X-ray structure of the K185A mutant of WbpE (WlbE) from pseudomonas aeruginosa in complex with PLP at 1.45 angstrom resolution==
-<StructureSection load='3nys' size='340' side='right' caption='[[3nys]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
+<StructureSection load='3nys' size='340' side='right'caption='[[3nys]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3nys]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NYS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NYS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3nys]] is a 1 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=3NYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NYS FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 1.45&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nyt|3nyt]], [[3nyu|3nyu]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=3nys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nys OCA], [http://pdbe.org/3nys PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nys RCSB], [http://www.ebi.ac.uk/pdbsum/3nys PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nys 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=3nys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nys OCA], [https://pdbe.org/3nys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nys RCSB], [https://www.ebi.ac.uk/pdbsum/3nys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nys ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ny/3nys_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ny/3nys_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Aminotransferase|Aminotransferase]]
+*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </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]]

3nys

From Proteopedia

Current revision

X-ray structure of the K185A mutant of WbpE (WlbE) from pseudomonas aeruginosa in complex with PLP at 1.45 angstrom resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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