Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins
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The porinologist.Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralisStructure, function, and evolution of bacterial ATP-binding cassette systemsThermodynamics of ABC transportersThe crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation.Crystal structure of a defective folding proteinInsights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutantsThe backbone structure of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein is essentially identical to its mesophilic E. coli homologStructural Analysis of a Periplasmic Binding Protein in the Tripartite ATP-independent Transporter Family Reveals a Tetrameric Assembly That May Have a Role in Ligand TransportCrystal structures of the choline/acetylcholine substrate-binding protein ChoX from Sinorhizobium meliloti in the liganded and unliganded-closed statesLigand-induced conformational changes in a thermophilic ribose-binding proteinAlternating Access in Maltose Transporter Mediated by Rigid-Body RotationsStructural analysis of the choline-binding protein ChoX in a semi-closed and ligand-free conformationStudies of the Maltose Transport System Reveal a Mechanism for Coupling ATP Hydrolysis to Substrate Translocation without Direct Recognition of SubstrateCrystal structure of the maltose transporter in a pretranslocation intermediate stateStructure determination of a sugar-binding protein from the phytopathogenic bacteriumXanthomonas citriPurification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubility, dimerization, and ATPase activityMaltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulationStructures of membrane proteins.Stimulation of the maltose transporter ATPase by unliganded maltose binding proteinSolution NMR studies of periplasmic binding proteins and their interaction partnersThe detergent-soluble maltose transporter is activated by maltose binding protein and verapamil.Maltose and maltodextrin transport in the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius is mediated by a high-affinity transport system that includes a maltose binding protein tolerant to low pH.Grappling archaea: ultrastructural analyses of an uncultivated, cold-loving archaeon, and its biofilm.Molecular genetic analysis of a locus required for resistance to antimicrobial peptides in Salmonella typhimuriumTrapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport.The tripartite ATP-independent periplasmic (TRAP) transporters of bacteria and archaea.Dynamics of alpha-helical subdomain rotation in the intact maltose ATP-binding cassette transporterUncoupling substrate transport from ATP hydrolysis in the Escherichia coli maltose transporter.Structural diversity of ABC transporters.Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transportersSalmonella enterica serovar enteritidis antimicrobial peptide resistance genes aid in defense against chicken innate immunity, fecal shedding, and egg depositionABC transporters: one, two or four extracytoplasmic substrate-binding sites?In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes.Nisin stimulates oxygen consumption by Staphylococcus aureus and Escherichia coli.Structural basis for substrate specificity of an amino acid ABC transporter.Characterization of transmembrane domains 6, 7, and 8 of MalF by mutational analysisUnliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system.How do ABC transporters drive transport?The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface.
P2860
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P2860
Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Mechanism of maltose transport ...... y periplasmic binding proteins
@en
type
label
Mechanism of maltose transport ...... y periplasmic binding proteins
@en
prefLabel
Mechanism of maltose transport ...... y periplasmic binding proteins
@en
P2093
P2860
P356
P1476
Mechanism of maltose transport ...... y periplasmic binding proteins
@en
P2093
A L Davidson
H A Shuman
P2860
P304
P356
10.1073/PNAS.89.6.2360
P407
P577
1992-03-01T00:00:00Z