Related ArticlesGating Mechanism of Aquaporin Z in Synthetic Bilayers and Native Membranes Revealed by Solid-state NMR Spectroscopy.
J Am Chem Soc. 2018 May 25;:
Authors: Zhao Y, Xie H, Wang L, Shen Y, Chen W, Song B, Zhang Z, Zheng A, Lin Q, Fu R, Wang J, Yang J
Abstract
Aquaporin Z (AqpZ) is an integral membrane protein that facilitates transport of water across E. coli cells with a high rate. Previously, R189, a highly conserved residue of the selective filter of AqpZ, was proposed as a gate within the water channel based on the observation of both open and closed conformations of its side-chain in different monomers of an X-ray structure, and the observation of rapid switches between the two conformations in molecular dynamic simulations. However, the gating mechanism of R189 side-chain remains controversial since it is unclear whether the different conformations observed in the X-ray structure is due to different functional states or is a result of perturbation of non-native detergent environments. Herein, in native-like synthetic bilayers and native E. coli membranes, a number of solid-state NMR techniques are employed to examine gating mechanism of R189 side-chain of AqpZ. One R189 side-chain conformation is highly evident since only a set of peaks corresponding to R189 side-chain is observed in 2D 15N-13C spectra. The immobility of R189 side-chain is detected by 1H-15N dipolar lineshapes, excluding the possibility of the rapid switches between the two side-chain conformations. High-resolution monomeric structure of AqpZ, determined by CS-Rosetta calculations using experimentally measured distance restraints related to R189 side-chain, reveals that this side-chain is in an open conformation, which is further verified by its water accessibility. All the solid-state NMR experimental results, combining with water permeability essay, suggest a permanently open conformation of R189 side-chain in the synthetic bilayer and native membranes. This study provides new structural insights into the gating mechanism of aquaporins and highlights the significance of lipid bilayer environments in elucidating the molecular mechanism of membrane proteins.
PMID: 29799200 [PubMed - as supplied by publisher]
[NMR paper] Studying the assembly of the BAM complex in native membranes by cellular solid-state NMR spectroscopy.
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J Struct Biol. 2017 Nov 29;:
Authors: Pinto C, Mance D, Julien M, Daniels M, Weingarth M, Baldus M
Abstract
Significant progress has been made in obtaining a structural insight into the assembly of the ?-barrel assembly machinery complex (BAM). These crystallography and electron microscopy studies used detergent as a membrane...
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Authors: Chen Y, Zhang Z, Tang X, Li J, Glaubitz C, Yang J
Abstract
Solid-state NMR is a powerful tool for studying membrane proteins in a native-like lipid environment. 3D magic angle spinning (MAS) NMR was employed to characterize the structure of E.coli diacylglycerol...
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04-06-2014 02:01 AM
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http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles The G-Protein-Coupled Neuropeptide Y Receptor Type 2 is Highly Dynamic in Lipid Membranes as Revealed by Solid-State NMR Spectroscopy.
Chemistry. 2014 Mar 13;
Authors: Schmidt P, Thomas L, Müller P, Scheidt HA, Huster D
Abstract
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[NMR paper] Investigation of the mechanism of action of novel amphipathic peptides: Insights from solid-state NMR studies of oriented lipid bilayers.
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Biochim Biophys Acta. 2014 Feb 6;
Authors: Fillion M, Noël M, Lorin A, Voyer N, Auger M
Abstract
We have investigated in the present study the effect of both non-selective and selective cationic 14-mer peptides on the lipid orientation of DMPC bilayers...
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02-11-2014 09:58 PM
[NMR paper] Aggregation and dynamics of oligocholate transporters in phospholipid bilayers revealed by solid-state NMR spectroscopy.
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Langmuir. 2012 Dec 11;28(49):17071-8
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Abstract
Macrocycles made of cholate building blocks were previously found to...
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05-22-2013 04:43 PM
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
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J Am Chem Soc. 2011 Jul 21;
Authors: Fu R, Wang X, Li C, Santiago-Miranda AN, Pielak GJ, Tian F
The feasibility of using solid state MAS NMR for in situ structural characterization of the LR11 (sorLA) transmembrane domain in native Escherichia coli (E. coli) membranes is presented. LR11 interacts with...
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Solid-State (19)F-NMR of Peptides in Native Membranes.
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Top Curr Chem. 2011 May 20;
Authors: Koch K, Afonin S, Ieronimo M, Berditsch M, Ulrich AS
To understand how membrane-active peptides (MAPs) function in vivo, it is essential to obtain structural information about them in their membrane-bound state. Most biophysical approaches rely on the use of bilayers prepared from synthetic phospholipids, i.e. artificial model membranes. A particularly successful structural method is solid-state NMR,...
Gating Mechanism of Aquaporin Z in Synthetic Bilayers and Native Membranes Revealed by Solid-state NMR Spectroscopy.
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