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  • 1
    Online Resource
    Online Resource
    San Diego :Elsevier Science & Technology,
    Keywords: Biological transport. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (957 pages)
    Edition: 1st ed.
    ISBN: 9780080543215
    Series Statement: Issn Series ; v.Volume 2
    Language: English
    Note: Cover -- Contents of Volume 2 -- General Preface -- Preface -- Contributors -- Part 1: Primary Transport -- Ion pumps -- Chapter 1. ATP-coupled Pumps for Heavy Metals and Metalloids -- Chapter 2. Sodium lon Coupled F1F0 ATPases -- Chapter 3. F-Type H + ATPase (ATP Synthase): Catalytic Site and Energy Coupling -- Chapter 4. The Neurospora Plasma Membrane Proton Pump -- Chapter 5. Structure and Function of the Yeast Vacuolar Membrane H+-ATPase -- Multidrug resistance and export systems -- Chapter 6. Structure and Function of HlyB, the ABC-transporter Essential for Haemolysin Secretion from Escherichia coli -- Chapter 7. The P-Glycoprotein Family and Multidrug Resistance: An Overview -- Chapter 8. Multidrug Resistance in Prokaryotes: Molecular Mechanisms of Drug Efflux -- Part 2: Secondary Transport -- Substrate transport and exchangers -- Chapter 9. Molecular Genetic Analysis of Membrane Protein Topology -- Chapter 10. The Lactose Permease of Escherichia coli: Past, Present and Future -- Chapter 11. Secondary Transporters and Metabolic Energy Generation in Bacteria -- Chapter 12. Pi-Linked Anion Exchange in Bacteria: Biochemical and Molecular Studies of UhpT and Related Porters -- Chapter 13. Structure of the Erythrocyte Band 3 Anion Exchanger -- Chapter 14. Erythrocyte Sugar Transport -- Chapter 15. The Mediator of Thyroidal Iodide Accumulation: The Sodium/Iodide Symporter -- Chapter 16. The Vertebrate Na+/H + Exchangers: Structure, Expression and Hormonal Regulation -- Neurotransmitters -- Chapter 17. Biogenic Amine Transporters of the Plasma Membrane -- Chapter 18. From Multidrug Resistance to Vesicular Neurotransmitter Transport -- Chapter 19. Structure and Function of Sodium-Coupled Amino Acid Neurotransmitter Transporters -- Homeostasis -- Chapter 20. lntracellular pH: Measurement, Manipulation and Physiological Regulation. , Chapter 21. K + Circulation Across the Prokaryotic Cell Membrane: K+-uptake Systems -- Chapter 22. Bacterial Na+/H + Antiporters - Molecular Biology, Biochemistry and Physiology -- Part 3: Phosphotransferase Systems -- Chapter 23. Biophysical Aspects of Carbohydrate Transport Regulation in Bacteria -- Chapter 24. Domain and Subunit Interactions and Their Role in the Function of the E. coli mannitol transporter, Eli MTL -- Chapter 25. Phosphotransferase Systems or PTSs as Carbohydrate Transport and as Signal Transduction Systems -- Part 4: Channels and Porines -- Chapter 26. lon Selectivity and Substrate Specificity: The Structural Basis of Porin Function -- Chapter 27. Intrinsic and Extrinsic Channels in Bacteria -- Chapter 28. Communication Between Membranes in TonB-Dependent Transport Across the Bacterial Outer Membrane -- Chapter 29. Colicin Transport, Channel Formation and Inhibition -- Chapter 30. Bacterial Ion Channels -- Part 5: Macromolecule Transport -- Chapter 31. Transport of DNA Through Bacterial Membranes -- Chapter 32. Translocation of Proteins Across the Bacterial Cytoplasmic Membrane -- Chapter 33. Protein Transport Across the Outer and Inner Membranes of Mitochondria -- Author lndex -- Subject Index.
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  • 2
    Publication Date: 2013-04-10
    Description: Major facilitator superfamily (MFS) transport proteins are ubiquitous in the membranes of all living cells, and ∼25% of prokaryotic membrane transport proteins belong to this superfamily. The MFS represents the largest and most diverse group of transporters and includes members that are clinically important. A wide range of substrates is...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 3
    Publication Date: 2013-05-29
    Description: Trp replacements for conserved Gly–Gly pairs between the N- and C-terminal six-helix bundles on the periplasmic side of lactose permease (LacY) cause complete loss of transport activity with little or no effect on sugar binding. Moreover, the detergent-solubilized mutants exhibit much greater thermal stability than WT LacY. A Cys replacement...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 4
    Publication Date: 2015-07-22
    Description: The X-ray crystal structure of a conformationally constrained mutant of the Escherichia coli lactose permease (the LacY double-Trp mutant Gly-46→Trp/Gly-262→Trp) with bound p-nitrophenyl-α-d-galactopyranoside (α-NPG), a high-affinity lactose analog, is described. With the exception of Glu-126 (helix IV), side chains Trp-151 (helix V), Glu-269 (helix VIII), Arg-144 (helix V), His-322 (helix...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 5
    Publication Date: 2016-11-02
    Description: The lactose permease of Escherichia coli (LacY), a dynamic polytopic membrane protein, catalyzes galactoside–H+ symport and operates by an alternating access mechanism that exhibits multiple conformations, the distribution of which is altered by sugar binding. We have developed single-domain camelid nanobodies (Nbs) against a mutant in an outward (periplasmic)-open conformation...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 6
    Publication Date: 2013-12-11
    Description: One fundamentally important problem for understanding the mechanism of coupling between substrate and H+ translocation with secondary active transport proteins is the identification and physical localization of residues involved in substrate and H+ binding. This information is exceptionally difficult to obtain with the Major Facilitator Superfamily (MFS) because of the...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 7
    Publication Date: 2014-02-05
    Description: Here we describe the X-ray crystal structure of a double-Trp mutant (Gly46→Trp/Gly262→Trp) of the lactose permease of Escherichia coli (LacY) with a bound, high-affinity lactose analog. Although thought to be arrested in an open-outward conformation, the structure is almost occluded and is partially open to the periplasmic side; the cytoplasmic...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 8
    Publication Date: 2014-04-23
    Description: The lactose permease (LacY) of Escherichia coli, a paradigm for the major facilitator superfamily, catalyzes the coupled stoichiometric translocation of a galactopyranoside and an H+ across the cytoplasmic membrane. To catalyze transport, LacY undergoes large conformational changes that allow alternating access of sugar- and H+-binding sites to either side of...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 9
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    The American Society for Biochemistry and Molecular Biology (ASBMB)
    Publication Date: 2013-09-28
    Description: To understand how YidC and SecYEG function together in membrane protein topogenesis, insertion and folding of the lactose permease of Escherichia coli (LacY), a 12-transmembrane helix protein LacY that catalyzes symport of a galactoside and an H+, was studied. Although both the SecYEG machinery and signal recognition particle are required for insertion of LacY into the membrane, YidC is not required for translocation of the six periplasmic loops in LacY. Rather, YidC acts as a chaperone, facilitating LacY folding. Upon YidC depletion, the conformation of LacY is perturbed, as judged by monoclonal antibody binding studies and by in vivo cross-linking between introduced Cys pairs. Disulfide cross-linking also demonstrates that YidC interacts with multiple transmembrane segments of LacY during membrane biogenesis. Moreover, YidC is strictly required for insertion of M13 procoat protein fused into the middle cytoplasmic loop of LacY. In contrast, the loops preceding and following the inserted procoat domain are dependent on SecYEG for insertion. These studies demonstrate close cooperation between the two complexes in membrane biogenesis and that YidC functions primarily as a foldase for LacY.
    Print ISSN: 0021-9258
    Electronic ISSN: 1083-351X
    Topics: Biology , Chemistry and Pharmacology
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  • 10
    Publication Date: 2012-03-21
    Description: LacY mutant Cys154 → Gly exhibits a periplasmic-closed crystal structure identical to the WT, but is periplasmic-open in the membrane. The mutant hardly catalyzes transport, but binds galactosides from either side of the membrane with the same affinity and is resistant to site-directed proteolysis relative to the pseudo-WT. Site-directed alkylation was also applied to 11 single-Cys mutants in Cys154 → Gly LacY in right-side-out membrane vesicles or after solubilization and purification in dodecyl-β-D-maltopyranoside (DDM). Unlike the pseudo-WT, Cys replacements on the periplasmic side of the Cys154 → Gly mutant label rapidly in the membrane without sugar, but labeling decreases markedly after the mutant proteins are purified. Thus, Cys154 → Gly LacY likely favors a higher-energy intermediate periplasmic-open conformation in situ, but collapses to a lower-energy periplasmic-closed conformation in DDM after purification. Notably, branched-chain or neopentyl glycol maltoside detergents stabilize Cys154 → Gly LacY in the membrane-embedded form.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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