2iv7

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of WaaG, a glycosyltransferase involved in lipopolysaccharide biosynthesis

Structural highlights

2iv7 is a 1 chain structure with sequence from Escherichia coli str. K-12 substr. W3110. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.6Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

WAAG_ECOLI Glucosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS) (PubMed:10986272, PubMed:24479701). Catalyzes the addition of the first outer-core glucose from UDP-glucose to the inner-core heptose II (PubMed:24479701). Cannot use other sugar donors, such as UDP-galactose, UDP-glucuronic acid, UDP-galacuronic acid, GDP-mannose, ADP-glucose and GDP-glucose (PubMed:24479701). In the absence of a lipid acceptor, can slowly hydrolyze UDP-glucose (PubMed:24479701).^[1] ^[2]

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

Glycosyltransferases (GTs) catalyze the synthesis of the myriad glycoconjugates that are central to life. One of the largest families is GT4, which contains several enzymes of therapeutic significance, exemplified by WaaG and AviGT4. WaaG catalyses a key step in lipopolysaccharide synthesis, while AviGT4, produced by Streptomyces viridochromogenes, contributes to the synthesis of the antibiotic avilamycin A. Here we present the crystal structure of both WaaG and AviGT4. The two enzymes contain two "Rossmann-like" (beta/alpha/beta) domains characteristic of the GT-B fold. Both recognition of the donor substrate and the catalytic machinery is similar to other retaining GTs that display the GT-B fold. Structural information is discussed with respect to the evolution of GTs and the therapeutic significance of the two enzymes.

Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4.,Martinez-Fleites C, Proctor M, Roberts S, Bolam DN, Gilbert HJ, Davies GJ Chem Biol. 2006 Nov;13(11):1143-52. PMID:17113996^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yethon JA, Vinogradov E, Perry MB, Whitfield C. Mutation of the lipopolysaccharide core glycosyltransferase encoded by waaG destabilizes the outer membrane of Escherichia coli by interfering with core phosphorylation. J Bacteriol. 2000 Oct;182(19):5620-3. PMID:10986272 doi:10.1128/JB.182.19.5620-5623.2000
↑ Qian J, Garrett TA, Raetz CR. In vitro assembly of the outer core of the lipopolysaccharide from Escherichia coli K-12 and Salmonella typhimurium. Biochemistry. 2014 Mar 4;53(8):1250-62. PMID:24479701 doi:10.1021/bi4015665
↑ Martinez-Fleites C, Proctor M, Roberts S, Bolam DN, Gilbert HJ, Davies GJ. Insights into the synthesis of lipopolysaccharide and antibiotics through the structures of two retaining glycosyltransferases from family GT4. Chem Biol. 2006 Nov;13(11):1143-52. PMID:17113996 doi:http://dx.doi.org/10.1016/j.chembiol.2006.09.005

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/2iv7"

@@ Line 3: / Line 3: @@
 <StructureSection load='2iv7' size='340' side='right'caption='[[2iv7]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2iv7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecow3 Ecow3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IV7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2iv7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._W3110 Escherichia coli str. K-12 substr. W3110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IV7 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]] 1.6&#8491;</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2iw1|2iw1]]</div></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=2iv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iv7 OCA], [https://pdbe.org/2iv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iv7 RCSB], [https://www.ebi.ac.uk/pdbsum/2iv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iv7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/RFAG_ECOLI RFAG_ECOLI]] Involved in the addition of the first glucose residue to the lipopolysaccharide core.
+[https://www.uniprot.org/uniprot/WAAG_ECOLI WAAG_ECOLI] Glucosyltransferase involved in the biosynthesis of the core oligosaccharide region of lipopolysaccharide (LPS) (PubMed:10986272, PubMed:24479701). Catalyzes the addition of the first outer-core glucose from UDP-glucose to the inner-core heptose II (PubMed:24479701). Cannot use other sugar donors, such as UDP-galactose, UDP-glucuronic acid, UDP-galacuronic acid, GDP-mannose, ADP-glucose and GDP-glucose (PubMed:24479701). In the absence of a lipid acceptor, can slowly hydrolyze UDP-glucose (PubMed:24479701).<ref>PMID:10986272</ref> <ref>PMID:24479701</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 16: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iv/2iv7_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Ecow3]]
+[[Category: Escherichia coli str. K-12 substr. W3110]]
 [[Category: Large Structures]]
-[[Category: Bolam, D N]]
+[[Category: Bolam DN]]
-[[Category: Davies, G J]]
+[[Category: Davies GJ]]
-[[Category: Gilbert, H J]]
+[[Category: Gilbert HJ]]
-[[Category: Martinez-Fleites, C]]
+[[Category: Martinez-Fleites C]]
-[[Category: Proctor, M]]
+[[Category: Proctor M]]
-[[Category: Roberts, S]]
+[[Category: Roberts S]]
-[[Category: Family gt-4]]
-[[Category: Glycosyltransferase]]
-[[Category: Lipopolysaccharide biosynthesis]]
-[[Category: Lp]]
-[[Category: Transferase]]

2iv7

From Proteopedia

Current revision

Crystal Structure of WaaG, a glycosyltransferase involved in lipopolysaccharide biosynthesis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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