onr:"swepub:oai:DiVA.org:su-220488"
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- Patrick, Joan,1987-Stockholms universitet,Institutionen för biokemi och biofysik,Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden (author)
Lipid- and substrate-induced conformational and dynamic changes in a glycosyltransferase involved in E. coli LPS synthesis revealed by 19F and 31P NMR
- Article/chapterEnglish2023
Publisher, publication year, extent ...
- Elsevier,2023
- printrdacarrier
Numbers
- LIBRIS-ID:oai:DiVA.org:su-220488
- https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-220488URI
- https://doi.org/10.1016/j.bbamem.2023.184209DOI
- https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-214262URI
Supplementary language notes
- Language:English
- Summary in:English
Part of subdatabase
- SwePubSwePub
Classification
Notes
- 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.
Subject headings and genre
- 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
- glycosyltransferase
- membrane interaction
- substrate interaction
- solution NMR
- bicelle
- lipids
- Biophysics
- biofysik
Added entries (persons, corporate bodies, meetings, titles ...)
- Pettersson, Pontus,1987-Stockholms universitet,Institutionen för biokemi och biofysik,Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden(Swepub:su)pope7677 (author)
- Mäler, Lena,1965-Umeå universitet,Stockholms universitet,Institutionen för biokemi och biofysik,Umeå University, Sweden,Kemiska institutionen,Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden(Swepub:umu)lema0099 (author)
- Stockholms universitetInstitutionen för biokemi och biofysik (creator_code:org_t)
Related titles
- In:Biochimica et Biophysica Acta - Biomembranes: Elsevier1865:80005-27361879-2642
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