about
The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-pSolution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIAGlucose of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase systemSolution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the Escherichia coli phosphotransferase systemSolution structure of the phosphoryl transfer complex between the signal-transducing protein IIAGlucose and the cytoplasmic domain of the glucose transporter IICBGlucose of the Escherichia coli glucose phosphotransferase systemSolution structure of the N-terminal amphitropic domain ofEscherichia coliglucose-specific enzyme IIA in membrane-mimetic micellesImportance of the carboxyl-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system for phosphoryl donor specificity.Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.Tautomeric state and pKa of the phosphorylated active site histidine in the N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system.How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteriaPhosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis.Demonstration of protein-protein interaction specificity by NMR chemical shift mapping.Investigation of a side-chain-side-chain hydrogen bond by mutagenesis, thermodynamics, and NMR spectroscopyThree-dimensional solution structure of the cytoplasmic B domain of the mannitol transporter IImannitol of the Escherichia coli phosphotransferase system.Induction of flexibility through protein-protein interactions.
P2860
Q27619116-98521556-921D-4BF9-AC8E-5B4726F9FB0BQ27627801-6B168331-84E0-4311-8F63-A04B6FFB2CEFQ27639553-2F3C4487-4C50-41EF-A3A5-7DDCAD62AFB2Q27641064-5C93BCD6-962F-42AD-86E2-BFBEFC1BDC60Q27641067-128F5787-FA04-455F-8A69-EF50DD69342CQ33621913-C7F89110-E1D9-4F9B-AB8D-16C4AC617A02Q34038287-5B170219-1691-4925-A6AA-40E8CA2B9E0FQ36280869-90F6B414-B070-4E27-BC27-F27AB52F4784Q36678721-EA7AD592-15EA-4DA6-A8FE-B47A9232D207Q41914232-063200BF-84B9-412E-91AA-A7067A1DDA31Q42159768-0369EDF4-B92C-423C-BB45-0FC9509C9C09Q42844727-4245D40F-5FE8-4C75-B4AF-873DAD024A22Q44982146-06A1BC3C-0941-469A-8DFE-7C4843E13FD2Q46776717-83EC5DF4-D422-4FB4-B06D-FB3C402D3E85
P2860
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh
1994年學術文章
@zh-hant
name
Unraveling a bacterial hexose transport pathway.
@en
type
label
Unraveling a bacterial hexose transport pathway.
@en
prefLabel
Unraveling a bacterial hexose transport pathway.
@en
P1476
Unraveling a bacterial hexose transport pathway
@en
P2093
P304
P356
10.1016/0959-440X(94)90262-3
P577
1994-12-01T00:00:00Z