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Lipid- and substrat...
Lipid- and substrate-induced conformational and dynamic changes in a glycosyltransferase involved in E. coli LPS synthesis revealed by 19F and 31P NMR
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- Patrick, Joan, 1987- (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden
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- Pettersson, Pontus, 1987- (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden
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- Mäler, Lena, 1965- (författare)
- Umeå universitet,Stockholms universitet,Institutionen för biokemi och biofysik,Umeå University, Sweden,Kemiska institutionen,Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden
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(creator_code:org_t)
- Elsevier, 2023
- 2023
- Engelska.
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Ingår i: Biochimica et Biophysica Acta - Biomembranes. - : Elsevier. - 0005-2736 .- 1879-2642. ; 1865:8
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Abstract
Ämnesord
Stäng
- WaaG is a glycosyltransferase (GT) involved in the synthesis of the bacterial cell wall, and in Escherichia coli it catalyzes the transfer of a glucose moiety from the donor substrate UDP-glucose onto the nascent lipopolysaccharide (LPS) molecule which when completed constitutes the major component of the bacterium's outermost defenses. Similar to other GTs of the GT-B fold, having two Rossman-like domains connected by a short linker, WaaG is believed to undergo complex inter-domain motions as part of its function to accommodate the nascent LPS and UDP-glucose in the catalytic site located in the cleft between the two domains. As the nascent LPS is bulky and membrane-bound, WaaG is a peripheral membrane protein, adding to the complexity of studying the enzyme in a biologically relevant environment. Using specific 5-fluoro-Trp labelling of native and inserted tryptophans and 19F NMR we herein studied the dynamic interactions of WaaG with lipids using bicelles, and with the donor substrate. Line-shape changes when bicelles are added to WaaG show that the dynamic behavior is altered when binding to the model membrane, while a chemical shift change indicates an altered environment around a tryptophan located in the C-terminal domain of WaaG upon interaction with UDP-glucose or UDP. A lipid-bound paramagnetic probe was used to confirm that the membrane interaction is mediated by a loop region located in the N-terminal domain. Furthermore, the hydrolysis of the donor substrate by WaaG was quantified by 31P NMR.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biofysik (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biophysics (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- glycosyltransferase
- membrane interaction
- substrate interaction
- solution NMR
- bicelle
- lipids
- Biophysics
- biofysik
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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