Zobrazeno 1 - 10
of 73
pro vyhledávání: '"Melibiose transport"'
Autor:
Lan Guan, Parameswaran Hariharan
The symporter melibiose permease MelB is the best-studied representative from MFS_2 family and the only protein in this large family with crystal structure determined. Previous thermodynamic studies show that MelB utilizes a cooperative binding as th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0caff9eb205c5b403dd03c54ef7e0fc5
https://doi.org/10.1101/2020.12.20.423627
https://doi.org/10.1101/2020.12.20.423627
Autor:
S G Shinnick, Manuel F. Varela
Publikováno v:
Journal of Membrane Biology. 189:191-199
Spontaneous mutants harboring the lacY gene on an F'-factor were isolated. Those mutants that failed to grow on 5 mM lactose minimal media plates were chosen for further study. The mutants showed striking mutations in the lactose carrier as well as i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::578010a6956a9ef020421fe36ae13361
https://doi.org/10.1007/s00232-002-1013-9
https://doi.org/10.1007/s00232-002-1013-9
Publikováno v:
Journal of bacteriology. 196(17)
The crystal structure of the Na + -coupled melibiose permease of Salmonella enterica serovar Typhimurium (MelB St ) demonstrates that MelB is a member of the major facilitator superfamily of transporters. Arg residues at positions 295, 141, and 363 a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7da56465408a683f6f454d075422dc1f
https://pubmed.ncbi.nlm.nih.gov/24957620
https://pubmed.ncbi.nlm.nih.gov/24957620
Publikováno v:
Biophysical Journal. 106(2)
The recently solved 3D crystal structures reveal that the Na+-coupled melibiose permease of Salmonella typhimurium (MelBSt) is a member of the Major Facilitator Superfamily (MFS). These inside-closed conformations show that Arg residues at positions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e15337800c4b4e92823dcb79ef112394
Autor:
Tomofusa Tsuchiya, Toshi Shimamoto, Xing-Jue Xu, Hideyuki Kawakami, Tadashi Shimamoto, Noriko Okazaki
Publikováno v:
Journal of Biochemistry. 129:607-613
Wild-type Citrobacter freundii cannot grow on melibiose as a sole source of carbon. The melibiose transporter gene melB was cloned from a C. freundii mutant M4 that could utilize melibiose as a sole carbon source. Although the cloned melB gene is clo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35fc637c1e331cd50c5c2a2e2be6e914
https://doi.org/10.1093/oxfordjournals.jbchem.a002897
https://doi.org/10.1093/oxfordjournals.jbchem.a002897
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1510:231-242
The melibiose carrier from Escherichia coli is a cation-substrate cotransporter that catalyzes the accumulation of galactosides at the expense of H(+), Na(+), or Li(+) electrochemical gradients. Charged residues on transmembrane domains in the amino-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c30b1460c4ee0a89d59774f4c196687b
https://doi.org/10.1016/s0005-2736(00)00353-9
https://doi.org/10.1016/s0005-2736(00)00353-9
Publikováno v:
Biochemistry. 39:4846-4854
The structural and functional consequences of a mismatch between the hydrophobic thickness d(P) of a transmembrane protein and that d(L) of the supporting lipid bilayer were investigated using melibiose permease (MelB) from Escherichia coli reconstit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f47a176a3ed31a95e415c1350faf0b3
https://doi.org/10.1021/bi992634s
https://doi.org/10.1021/bi992634s
Publikováno v:
Journal of Biological Chemistry. 273:33192-33197
Further insight into the cosubstrate-induced structural change of the melibiose permease (MelB) of Escherichia coli has been sought by investigating the binding and spectroscopic properties of the fluorescent sugar 2′-(N-5-dimethylaminonaphthalene-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0bdb97e209ad843556084afb9d06af9d
https://doi.org/10.1074/jbc.273.50.33192
https://doi.org/10.1074/jbc.273.50.33192
Autor:
C. van der Does, Gérard Leblanc, Berend Poolman, Jan Knol, Peter J. F. Henderson, Thierry Pourcher, Wei-Jun Liang, Isabelle Mus-Veteau
Publikováno v:
Molecular Microbiology. 19:911-922
A new family of homologous membrane proteins that transport galactosides-pentoses-hexuronides (GPH) is described, By analysing the aligned amino acid sequences of the GPH family, and by exploiting their different specificities for cations and sugars,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a9b53a64091cdefd371eace99372f95
https://doi.org/10.1046/j.1365-2958.1996.397949.x
https://doi.org/10.1046/j.1365-2958.1996.397949.x
Autor:
H Hama, T H Wilson
Publikováno v:
Journal of Biological Chemistry. 269:1063-1067
The melibiose carrier of Klebsiella pneumoniae couples sugar transport to H+ and Li+, while that of Escherichia coli uses Na+ besides the other two cation species (Hama and Wilson, 1992). We have shown that the K. pneumoniae melibiose carrier is capa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::893446d62b6577cb00b1712323830aa3
https://doi.org/10.1016/s0021-9258(17)42221-6
https://doi.org/10.1016/s0021-9258(17)42221-6