Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complex.

Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complex.

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http://www.wikidata.org/entity/Q38353484
The extreme C terminus of the ABC protein DrrA contains unique motifs involved in function and assembly of the DrrAB complexNucleotide-dependent dimerization of the C-terminal domain of the ABC transporter CvaB in colicin V secretion.P-glycoprotein retains drug-stimulated ATPase activity upon covalent linkage of the two nucleotide binding domains at their C-terminal ends.Role of dihydrolipoamide dehydrogenase in regulation of raffinose transport in Streptococcus pneumoniaeInvolvement of the carboxyl-terminal region of the yeast peroxisomal half ABC transporter Pxa2p in its interaction with Pxa1p and in transporter function.The ATPase activity of the P-glycoprotein drug pump is highly activated when the N-terminal and central regions of the nucleotide-binding domains are linked closely togetherFull engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporterHow phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteriaBoth maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporterCanonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.Molecular mechanism of the Escherichia coli maltose transporter.Topography of the surface of the signal-transducing protein EIIA(Glc) that interacts with the MalK subunits of the maltose ATP-binding cassette transporter (MalFGK2) of Salmonella typhimurium.The ABC transporter MalFGK(2) sequesters the MalT transcription factor at the membrane in the absence of cognate substrate.Binding Protein-Dependent Uptake of Maltose into Cells via an ATP-Binding Cassette Transporter.In vivo phosphorylation of CFTR promotes formation of a nucleotide-binding domain heterodimer.Structure of the ATPase subunit CysA of the putative sulfate ATP-binding cassette (ABC) transporter from Alicyclobacillus acidocaldarius.Carbohydrate kinase (RhaK)-dependent ABC transport of rhamnose in Rhizobium leguminosarum demonstrates genetic separation of kinase and transport activities.
P2860

Disulfide cross-linking reveals a site of stable interaction between C-terminal regulatory domains of the two MalK subunits in the maltose transport complex.

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http://www.wikidata.org/entity/Q38353484
description
2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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2003年学术文章
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name
Disulfide cross-linking reveal ...... the maltose transport complex.
@en
type
label
Disulfide cross-linking reveal ...... the maltose transport complex.
@en
prefLabel
Disulfide cross-linking reveal ...... the maltose transport complex.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Disulfide cross-linking reveal ...... the maltose transport complex.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698