Structure of a prokaryotic virtual proton pump at 3.2 A resolution.
Yiling Fang,Hariharan Jayaram,Tania Shane,Ludmila Kolmakova-Partensky,Fang Wu,Carole Williams,Yong Xiong,Christopher Miller +7 more
Reads0
Chats0
TLDR
A crystal structure of AdiC is described, which shows that the protein is captured in an outward-open, substrate-free conformation with transmembrane architecture remarkably similar to that seen in four other families of apparently unrelated transport proteins.Abstract:
To reach the mammalian gut, enteric bacteria must pass through the stomach. Many such organisms survive exposure to the harsh gastric environment (pH 1.5-4) by mounting extreme acid-resistance responses, one of which, the arginine-dependent system of Escherichia coli, has been studied at levels of cellular physiology, molecular genetics and protein biochemistry. This multiprotein system keeps the cytoplasm above pH 5 during acid challenge by continually pumping protons out of the cell using the free energy of arginine decarboxylation. At the heart of the process is a 'virtual proton pump' in the inner membrane, called AdiC, that imports L-arginine from the gastric juice and exports its decarboxylation product agmatine. AdiC belongs to the APC superfamily of membrane proteins, which transports amino acids, polyamines and organic cations in a multitude of biological roles, including delivery of arginine for nitric oxide synthesis, facilitation of insulin release from pancreatic beta-cells, and, when inappropriately overexpressed, provisioning of certain fast-growing neoplastic cells with amino acids. High-resolution structures and detailed transport mechanisms of APC transporters are currently unknown. Here we describe a crystal structure of AdiC at 3.2 A resolution. The protein is captured in an outward-open, substrate-free conformation with transmembrane architecture remarkably similar to that seen in four other families of apparently unrelated transport proteins.read more
Citations
More filters
Journal ArticleDOI
Biology of Human Sodium Glucose Transporters
TL;DR: A personal review of advances in the genetics, molecular biology, biochemistry, biophysics, and structure of SGLTs, including cotransporters for sugars, anions, vitamins, and short-chain fatty acids.
Journal ArticleDOI
SLC6 Neurotransmitter Transporters: Structure, Function, and Regulation
Anders S. Kristensen,Jacob Andersen,Trine Nygaard Jørgensen,Lena Sørensen,Jacob Eriksen,Claus J. Loland,Kristian Strømgaard,Ulrik Gether +7 more
TL;DR: The understanding of the molecular structure, function, and pharmacology of these proteins has advanced rapidly, and intensive efforts have been directed toward understanding the molecular and cellular mechanisms involved in regulation of the activity of this important class of transporters, leading to new methodological developments and important insights.
Journal ArticleDOI
The SLC3 and SLC7 families of amino acid transporters
TL;DR: The link between specific mutations in HATs and the primary inherited aminoacidurias, cystinuria and lysinuric protein intolerance is described.
Journal ArticleDOI
The ABCs of membrane transporters in health and disease (SLC series): Introduction
TL;DR: The existing online resource for solute carriers, the Bioparadigms SLC Tables, has been updated and significantly extended with additional information and cross-links to other relevant databases, and the nomenclature used in this database has been validated and approved by the HGNC.
Journal ArticleDOI
Crystal structure of a bacterial homologue of glucose transporters GLUT1–4
TL;DR: In this paper, X-ray crystal structures of XylE, an Escherichia coli xylose transporter, were reported, which is a bacterial homologue of the human glucose transporters GLUT1-4, complexed with glucose and its analogues.
References
More filters
Journal ArticleDOI
Improved Fourier coefficients for maps using phases from partial structures with errors
TL;DR: In this article, a method is given to estimate the parameter σA in these phase probability expressions from the observed and calculated structure factor amplitudes, from which one can estimate the mean coordinate error for the model, and when there are coordinate errors, a new expression for the non-centric Fourier coefficients is required to suppress this model bias.
Journal ArticleDOI
X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity.
TL;DR: This work presents the X-ray structures of two prokaryotic ClC Cl- channels from Salmonella enterica serovar typhimurium and Escherichia coli at 3.0 and 3.5 Å, respectively, and establishes the physical and chemical basis of their anion selectivity.
Journal ArticleDOI
Crystal structure of a bacterial homologue of na(+) cl(-)-dependent neurotransmitter transporters
James Gouaux,Atsuko Yamashita +1 more
TL;DR: The structure of a bacterial homologue of these transporters from Aquifex aeolicus, in complex with its substrate, leucine, and two sodium ions, is presented and reveals the architecture of this important class of transporter, illuminates the determinants of substrate binding and ion selectivity, and defines the external and internal gates.
Journal ArticleDOI
Structure of a glycerol-conducting channel and the basis for its selectivity.
Daxiong Fu,Andrew Libson,Larry J. W. Miercke,Weitzman C,Peter Nollert,J. Krucinski,Robert M. Stroud +6 more
TL;DR: The crystal structure of the Escherichia coli glycerol facilitator (GlpF) elucidates the mechanism of selective permeability for linear carbohydrates and suggests how ions and water are excluded.
Journal ArticleDOI
Escherichia coli acid resistance: tales of an amateur acidophile
TL;DR: Surprisingly, certain microorganisms that grow at neutral pH have elegantly regulated systems that enable survival during excursions into acidic environments, and the best-characterized acid-resistance system is found in E. coli.
Related Papers (5)
Crystal structure of a bacterial homologue of na(+) cl(-)-dependent neurotransmitter transporters
James Gouaux,Atsuko Yamashita +1 more
Structure and Molecular Mechanism of a Nucleobase-Cation-Symport-1 Family Transporter
Simone Weyand,Tatsuro Shimamura,Tatsuro Shimamura,Shunsuke Yajima,Shunichi Suzuki,Osman Mirza,Kuakarun Krusong,Elisabeth P. Carpenter,Nicholas G. Rutherford,Jonathan M. Hadden,John O'Reilly,Pikyee Ma,Massoud Saidijam,Massoud Saidijam,Simon G. Patching,Ryan J. Hope,Halina Norbertczak,Peter Roach,So Iwata,Peter J. F. Henderson,Alexander D. Cameron +20 more