The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface.
about
Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulationThe detergent-soluble maltose transporter is activated by maltose binding protein and verapamil.Interactions of VirB9, -10, and -11 with the membrane fraction of Agrobacterium tumefaciens: solubility studies provide evidence for tight associations.Evidence that KpsT, the ATP-binding component of an ATP-binding cassette transporter, is exposed to the periplasm and associates with polymer during translocation of the polysialic acid capsule of Escherichia coli K1In vitro disassembly and reassembly of an ABC transporter, the histidine permease.The Vibrio fischeri luminescence gene activator LuxR is a membrane-associated protein.Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocationP-glycoprotein structure and evolutionary homologies.The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane.Maltose transport system of Escherichia coli: an ABC-type transporter.Expression and purification of the first nucleotide-binding domain and linker region of human multidrug resistance gene product: comparison of fusions to glutathione S-transferase, thioredoxin and maltose-binding protein.In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: modulation by ATP.The ABC maltose transporter.Domain interactions in the yeast ATP binding cassette transporter Ycf1p: intragenic suppressor analysis of mutations in the nucleotide binding domainsThe SecA subunit of Escherichia coli preprotein translocase is exposed to the periplasm.A phosphate transport system is required for symbiotic nitrogen fixation by Rhizobium meliloti.The VirB4 ATPase of Agrobacterium tumefaciens is a cytoplasmic membrane protein exposed at the periplasmic surfaceCharacterization of membrane and protein interaction determinants of the Agrobacterium tumefaciens VirB11 ATPase.Structural insights into the secretin PulD and its trypsin-resistant core.Modulation of ATPase activity by physical disengagement of the ATP-binding domains of an ABC transporter, the histidine permease.One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease.Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex. Effect of different ligands and consequences for the mechanism of action.Endogenous SecA catalyzes preprotein translocation at SecYEG.Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis.Hemolysin transport in Escherichia coli. Point mutants in HlyB compensate for a deletion in the predicted amphiphilic helix region of the HlyA signal.
P2860
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P2860
The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
The ATP-binding component of a ...... eriplasmic (external) surface.
@ast
The ATP-binding component of a ...... eriplasmic (external) surface.
@en
type
label
The ATP-binding component of a ...... eriplasmic (external) surface.
@ast
The ATP-binding component of a ...... eriplasmic (external) surface.
@en
prefLabel
The ATP-binding component of a ...... eriplasmic (external) surface.
@ast
The ATP-binding component of a ...... eriplasmic (external) surface.
@en
P2093
P2860
P356
P1476
The ATP-binding component of a ...... eriplasmic (external) surface.
@en
P2093
P2860
P304
P356
10.1073/PNAS.90.2.620
P407
P577
1993-01-01T00:00:00Z