Molecular modeling and site-directed mutagenesis of plant chloroplast monogalactosyldiacylglycerol synthase reveal critical residues for activity
Result 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 aUDP-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 supportedby 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. Two short segments of MGD (beta2-alpha2
Keywords
The result's identifiers
Result code in IS VaVaI
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Molecular modeling and site-directed mutagenesis of plant chloroplast monogalactosyldiacylglycerol synthase reveal critical residues for activity
Original language 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 aUDP-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 supportedby 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. Two short segments of MGD (beta2-alpha2
Czech name
Molekulové modelování a místně cílená mutageneze MDGD synthasy rostlinného chloroplastu odhalují rezidua nezbytná pro její aktivitu
Czech description
Monogalaktosyldiacylglycerol (MGDG), hlavní složka rostlinných plastidů, je syntetizován MGDG synthasou (MGD) - glykosyltransferasou přítomnou v membráně plastidu, která katalyzuje přenos galaktosylové skupiny z UDP-galaktosy (donor) na diacylglycerol (akceptor). Zatím není dostupná žádná strukturní informace o tomto důležitém enzymu, který je vhodným cílem pro design herbicidů. S pomocí metod homologního modelování v této práci představujeme model MGDG synthasy ze špenátu, který byl vytvořen podle analogie s proteinem MURG z Escherichia coli, jehož rentgenová struktura je známa.
Classification
Type
Jx - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2005
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
J. Biol. Chem.
ISSN
0021-9258
e-ISSN
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Volume of the periodical
280
Issue of the periodical within the volume
41
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
34691-34701
UT code for WoS article
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EID of the result in the Scopus database
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Result type
Jx - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP
CE - Biochemistry
Year of implementation
2005