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Statements

Subject Item
n2:RIV%2F00216224%3A14110%2F05%3A00020163%21RIV10-GA0-14110___
rdf:type
n11:Vysledek skos:Concept
dcterms:description
Monogalactosyldiacylglycerol (MGDG), the major lipid of plant and algal plastids, is synthesized by MGD (or MGDG synthase), a dimeric and membrane-bound glycosyltransferase of the plastid envelope that catalyzes the transfer of a galactosyl group from a UDP-galactose donor onto a diacylglycerol acceptor. Although this enzyme is essential for biogenesis, and therefore an interesting target for herbicide design, no structural information is available. MGD monomers share sequence similarity with MURG, a bacterial glycosyltransferase catalyzing the transfer of N-acetyl-glucosamine on Lipid 1. Using the x-ray structure of Escherichia coli MURG as a template, we computed a model for the fold of Spinacia oleracea MGD. This structural prediction was supported by site-directed mutagenesis analyses. The predicted monomer architecture is a double Rossmann fold. The binding site for UDP-galactose was predicted in the cleft separating the two Rossmann folds. Monogalactosyldiacylglycerol (MGDG), the major lipid of plant and algal plastids, is synthesized by MGD (or MGDG synthase), a dimeric and membrane-bound glycosyltransferase of the plastid envelope that catalyzes the transfer of a galactosyl group from a UDP-galactose donor onto a diacylglycerol acceptor. Although this enzyme is essential for biogenesis, and therefore an interesting target for herbicide design, no structural information is available. MGD monomers share sequence similarity with MURG, a bacterial glycosyltransferase catalyzing the transfer of N-acetyl-glucosamine on Lipid 1. Using the x-ray structure of Escherichia coli MURG as a template, we computed a model for the fold of Spinacia oleracea MGD. This structural prediction was supported by site-directed mutagenesis analyses. The predicted monomer architecture is a double Rossmann fold. The binding site for UDP-galactose was predicted in the cleft separating the two Rossmann folds.
dcterms:title
Molecular modeling and site-directed mutagenesis of plant chloroplast monogalactosyldiacylglycerol synthase reveal critical residues for activity Molecular modeling and site-directed mutagenesis of plant chloroplast monogalactosyldiacylglycerol synthase reveal critical residues for activity
skos:prefLabel
Molecular modeling and site-directed mutagenesis of plant chloroplast monogalactosyldiacylglycerol synthase reveal critical residues for activity Molecular modeling and site-directed mutagenesis of plant chloroplast monogalactosyldiacylglycerol synthase reveal critical residues for activity
skos:notation
RIV/00216224:14110/05:00020163!RIV10-GA0-14110___
n3:aktivita
n6:P n6:Z
n3:aktivity
P(GD204/03/H016), Z(MSM0021622413)
n3:cisloPeriodika
41
n3:dodaniDat
n5:2010
n3:domaciTvurceVysledku
n15:1139002 n15:4347374
n3:druhVysledku
n8:J
n3:duvernostUdaju
n10:S
n3:entitaPredkladatele
n14:predkladatel
n3:idSjednocenehoVysledku
531018
n3:idVysledku
RIV/00216224:14110/05:00020163
n3:jazykVysledku
n19:eng
n3:klicovaSlova
glycosyltransferases; molecular modeling; MDGD synthase
n3:klicoveSlovo
n4:glycosyltransferases n4:MDGD%20synthase n4:molecular%20modeling
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[4DE1F3385CA7]
n3:nazevZdroje
J. Biol. Chem.
n3:obor
n13:CE
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
7
n3:projekt
n16:GD204%2F03%2FH016
n3:rokUplatneniVysledku
n5:2005
n3:svazekPeriodika
280
n3:tvurceVysledku
Šnajdrová, Lenka Breton, Christelle Botte, Cyrille Koča, Jaroslav Marechal, Eric Jeanneau, Charlotte Imberty, Anne
n3:zamer
n17:MSM0021622413
s:issn
0021-9258
s:numberOfPages
11
n18:organizacniJednotka
14110