Search results for: H. Ronald Kaback

Items from 1 to 20 out of 47 results

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Monoclonal antibody 4B1 influences the pK_a of Glu325 in lactose permease (LacY) from Escherichia coli: evidence from SEIRAS

Fatima Omeis, Ana Filipa Santos Seica, Natalia Ermolova, H. Ronald Kaback, more

The monoclonal antibody 4B1 binds to a conformational epitope on the periplasmic side of lactose permease (LacY) of Escherichia coli and inhibits H⁺/lactose symport and lactose efflux under nonenergized conditions. At the same time, ligand binding and translocation reactions that do not involve net H⁺ translocation remain unaffected by 4B1. In this study, surface‐enhanced infrared absorption spectroscopy...

article

Thermodynamic Insights into Conformational Dynamics of Sugar Transporters

Hariharan Parameswaran, Xiaoxu Jiang, Els Pardon, Jan Steyaert, more

Biophysical Journal > 2016 > 110 > 3 Supplement 1 > 137a

article

Observing a Lipid-Dependent Alteration in Single Lactose Permeases

Tetiana Serdiuk, Junichi Sugihara, Stefania A. Mari, H. Ronald Kaback, more

Structure > 2015 > 23 > 4 > 754-761

Lipids of the Escherichia coli membrane are mainly composed of 70%–80% phosphatidylethanolamine (PE) and 20%–25% phosphatidylglycerol (PG). Biochemical studies indicate that the depletion of PE causes inversion of the N-terminal helix bundle of the lactose permease (LacY), and helix VII becomes extramembranous. Here we study this phenomenon using single-molecule force spectroscopy, which is sensitive...

article

Proton-Coupled Dynamics in Lactose Permease

Magnus Andersson, Ana-Nicoleta Bondar, J. Alfredo Freites, Douglas J. Tobias, more

Structure > 2012 > 20 > 11 > 1893-1904

Lactose permease of Escherichia coli (LacY) catalyzes symport of a galactopyranoside and an H ⁺ via an alternating access mechanism. The transition from an inward- to an outward-facing conformation of LacY involves sugar-release followed by deprotonation. Because the transition depends intimately upon the dynamics of LacY in a bilayer environment, molecular dynamics (MD) simulations may be...

article

Lactose permease: A beautiful chemiosmotic machine

H. Ronald Kaback

BBA - Bioenergetics > 2012 > 1817 > Supplement > S1

article

Sugar Recognition by CscB and LacY

Junichi Sugihara, Irina Smirnova, Vladimir Kasho, H. Ronald Kaback

Biochemistry > 2011 > 50 > 51 > 11009 - 11014

article

Lactose Permease and the Alternating Access Mechanism

Irina Smirnova, Vladimir Kasho, H. Ronald Kaback

Biochemistry > 2011 > 50 > 45 > 9684 - 9693

article

Site-Directed Alkylation Studies with LacY Provide Evidence for the Alternating Access Model of Transport

Xiaoxu Jiang, Yiling Nie, H. Ronald Kaback

Biochemistry > 2011 > 50 > 10 > 1634 - 1640

article

The old Man and the Membrane

H. Ronald Kaback

Biophysical Journal > 2011 > 100 > 3 Supplement 1 > 513a

article

The Alternating Access Transport Mechanism in LacY

H. Ronald Kaback, Irina Smirnova, Vladimir Kasho, Yiling Nie, more

The Journal of Membrane Biology > 2011 > 239 > 1-2 > 85-93

Lactose permease of Escherichia coli (LacY) is highly dynamic, and sugar binding causes closing of a large inward-facing cavity with opening of a wide outward-facing hydrophilic cavity. Therefore, lactose/H⁺ symport via LacY very likely involves a global conformational change that allows alternating access of single sugar- and H⁺-binding sites to either side of the membrane. Here, in honor of Stephan...

article

Delineating Electrogenic Reactions during Lactose/H ⁺ Symport

Juan J. Garcia-Celma, Julian Ploch, Irina Smirnova, H. Ronald Kaback, more

Biochemistry > 2010 > 49 > 29 > 6115 - 6121

article

Helix Dynamics in LacY: Helices II and IV

Zhenyu Liu, M. Gregor Madej, H. Ronald Kaback

Journal of Molecular Biology > 2010 > 396 > 3 > 617-626

Biochemical and biophysical studies based upon crystal structures of both a mutant and wild-type lactose permease from Escherichia coli (LacY) in an inward-facing conformation have led to a model for the symport mechanism in which both sugar and H ⁺ binding sites are alternatively accessible to both sides of the membrane. Previous findings indicate that the face of helix II with Asp68 is important...

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Residues Gating the Periplasmic Pathway of LacY

Yonggang Zhou, Yiling Nie, H. Ronald Kaback

Journal of Molecular Biology > 2009 > 394 > 2 > 219-225

X-ray crystal structures of LacY (lactose permease of Escherichia coli) exhibit a large cytoplasmic cavity containing the residues involved in sugar binding and H ⁺ translocation at the apex and a tightly packed side facing the periplasm. However, biochemical and biophysical evidence provide a strong indication that a hydrophilic pathway opens on the external surface of LacY with closing of...

article

Properties of a LacY Efflux Mutant

Lan Guan, H. Ronald Kaback

Biochemistry > 2009 > 48 > 39 > 9250 - 9255

article

Residues in the H ⁺ Translocation Site Define the p K _a for Sugar Binding to LacY

Irina Smirnova, Vladimir Kasho, Junichi Sugihara, Jun-Yong Choe, more

Biochemistry > 2009 > 48 > 37 > 8852 - 8860

article

Clogging the Periplasmic Pathway in LacY ^†

Yiling Nie, Yonggang Zhou, H. Ronald Kaback

Biochemistry > 2009 > 48 > 4 > 738 - 743

article

2007 Annual progress report synopsis of the Center for Structures of Membrane Proteins

Robert M. Stroud, Senyon Choe, James Holton, H. Ronald Kaback, more

Journal of Structural and Functional Genomics > 2009 > 10 > 2 > 193-208

A synopsis of the 2007 annual progress report for the Center for Structures of Membrane Proteins, a specialized center of the Protein Structure Initiative.

article

The Cys154→Gly Mutation in LacY Causes Constitutive Opening of the Hydrophilic Periplasmic Pathway

Yiling Nie, Frances E. Sabetfard, H. Ronald Kaback

Journal of Molecular Biology > 2008 > 379 > 4 > 695-703

The lactose permease of Escherichia coli (LacY) is a highly dynamic membrane transport protein, while the Cys154→Gly mutant is crippled conformationally. The mutant binds sugar with high affinity, but catalyzes very little translocation across the membrane. In order to further investigate the defect in the mutant, fluorescent maleimides were used to examine the accessibility/reactivity of single-Cys...

article

Site-directed Alkylation of LacY: Effect of the Proton Electrochemical Gradient

Yiling Nie, Natalia Ermolova, H. Ronald Kaback

Journal of Molecular Biology > 2007 > 374 > 2 > 356-364

Previous N-ethylmaleimide-labeling studies show that ligand binding increases the reactivity of single-Cys mutants located predominantly on the periplasmic side of LacY and decreases reactivity of mutants located for the most part of the cytoplasmic side. Thus, sugar binding appears to induce opening of a periplasmic pathway with closing of the cytoplasmic cavity resulting in alternative access of...

article

Direct Sugar Binding to LacY Measured by Resonance Energy Transfer ^†

Irina N. Smirnova, Vladimir N. Kasho, H. Ronald Kaback

Biochemistry > 2006 > 45 > 51 > 15279 - 15287

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INFONA - science communication portal

Search results for: H. Ronald Kaback

Monoclonal antibody 4B1 influences the pK_a of Glu325 in lactose permease (LacY) from Escherichia coli: evidence from SEIRAS

Thermodynamic Insights into Conformational Dynamics of Sugar Transporters

Observing a Lipid-Dependent Alteration in Single Lactose Permeases

Proton-Coupled Dynamics in Lactose Permease

Lactose permease: A beautiful chemiosmotic machine

Sugar Recognition by CscB and LacY

Lactose Permease and the Alternating Access Mechanism

Site-Directed Alkylation Studies with LacY Provide Evidence for the Alternating Access Model of Transport

The old Man and the Membrane

The Alternating Access Transport Mechanism in LacY

Delineating Electrogenic Reactions during Lactose/H ⁺ Symport

Helix Dynamics in LacY: Helices II and IV

Residues Gating the Periplasmic Pathway of LacY

Properties of a LacY Efflux Mutant

Residues in the H ⁺ Translocation Site Define the p K _a for Sugar Binding to LacY

Clogging the Periplasmic Pathway in LacY ^†

2007 Annual progress report synopsis of the Center for Structures of Membrane Proteins

The Cys154→Gly Mutation in LacY Causes Constitutive Opening of the Hydrophilic Periplasmic Pathway

Site-directed Alkylation of LacY: Effect of the Proton Electrochemical Gradient

Direct Sugar Binding to LacY Measured by Resonance Energy Transfer ^†

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