Physiological evidence for an interaction between helices II and XI in the melibiose carrier of Escherichia coli.
TLDR
It is suggested that Asp-59 and Lys-377 interact via a salt bridge that brings helix II and helix XI close to one another in the three-dimensional structure of the carrier.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 2001-02-09 and is currently open access. It has received 19 citations till now. The article focuses on the topics: Melibiose transport & Melibiose.read more
Citations
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Journal ArticleDOI
A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin
Jan H. Reiling,Clary B. Clish,Jan E. Carette,Jan E. Carette,Malini Varadarajan,Thijn R. Brummelkamp,Thijn R. Brummelkamp,David M. Sabatini +7 more
TL;DR: A critical role is uncovered for MFSD2A by acting as a putative TM transporter at the plasma membrane by identifying transmembrane helical amino acid residues essential for mediating TM sensitivity.
Journal ArticleDOI
Mechanism of melibiose/cation symport of the melibiose permease of Salmonella typhimurium.
TL;DR: FRET studies show symmetrical emission maximum at ∼500 nm with MelB-ST in the presence of 2′-(N-dansyl)aminoalkyl-1-thio-β-d-galactopyranoside and Na+, Li+, or H+, which implies a relatively homogeneous distribution of conformers of MelB -ST ternary complexes in the membrane.
Journal ArticleDOI
Structural Insights into the Transport Mechanism of the Human Sodium-dependent Lysophosphatidylcholine Transporter MFSD2A
TL;DR: Three three-dimensional structural models of human MFSD2A derived by homology modeling using MelB- and LacY-based crystal structures and refined by biochemical analysis support a novel transport mechanism by which lysophosphatidylcholines are “flipped” within the transporter cavity by pivoting about Lys-436 leading to net transport from the outer to the inner leaflet of the plasma membrane.
Journal ArticleDOI
APH1 Polar Transmembrane Residues Regulate the Assembly and Activity of Presenilin Complexes
Raphaëlle Pardossi-Piquard,Seung Pil Yang,Soshi Kanemoto,Yongjun Gu,Fusheng Chen,Christopher Bohm,Jean Sevalle,Tong Li,Philip C. Wong,Frédéric Checler,Gerold Schmitt-Ulms,Peter St George-Hyslop,Peter St George-Hyslop,Paul E. Fraser +13 more
TL;DR: The results suggest that the conserved transmembrane histidine residues contribute to APH1 function and can affect presenilin catalytic activity.
Journal ArticleDOI
A 3D structure model of the melibiose permease of Escherichia coli represents a distinctive fold for Na+ symporters
Mohammad S. Yousef,Lan Guan +1 more
TL;DR: The proposed overall fold of MelB is different from the available crystal structures of other Na+-coupled transporters, suggesting a distinctive fold for Na+ symporters.
References
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Journal ArticleDOI
Structure and function of voltage-sensitive ion channels
TL;DR: Experimental results have begun to define a functional map of voltage-sensitive Na+ and Ca2+ channels, and coordinated application of biochemical, biophysical, and molecular genetic methods should lead to a clear understanding of the molecular basis of electrical excitability.
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Carbohydrate-binding proteins: tertiary structures and protein-sugar interactions.
TL;DR: The structure of sugar-Induced Conformational Change in Proteins and its effects on Binding Sites and Bonds and van der Waals Contacts are illustrated.
Journal ArticleDOI
Cys-scanning mutagenesis: a novel approach to structure–function relationships in polytopic membrane proteins
TL;DR: The entire lactose permease of Escherichia coli, a polytopic membrane transport protein that catalyzes β‐galactoside/H+ symport, has been subjected to Cys‐scanning mutagenesis to determine which residues play an obligatory role in the mechanism and to create a library of mutants with a single‐Cys residue at each position of the molecule for structure/function studies.
Journal ArticleDOI
Lactose transport coupled to proton movements in Escherichia coli.
TL;DR: Evidence of a flow of protons into Escherichia coli when lactose is transported inwards by the lactose carrier is given.
Journal ArticleDOI
Cation and sugar selectivity determinants in a novel family of transport proteins
Berend Poolman,Jan Knol,C. van der Does,Wei-Jun Liang,Peter J. F. Henderson,Gérard Leblanc,Thierry Pourcher,Isabelle Mus-Veteau +7 more
TL;DR: In this article, a new family of homologous membrane proteins that transport galactosides-pentoses-hexuronides (GPH) is described, by analysing the aligned amino acid sequences of the GPH family, and by exploiting their different specificities for cations and sugars.