Related ArticlesMechanisms of proton conduction and gating in influenza m2 proton channels from solid-state NMR.
Science. 2010 Oct 22;330(6003):505-8
Authors: Hu F, Luo W, Hong M
The M2 protein of influenza viruses forms an acid-activated tetrameric proton channel. We used solid-state nuclear magnetic resonance spectroscopy to determine the structure and functional dynamics of the pH-sensing and proton-selective histidine-37 in M2 bound to a cholesterol-containing virus-envelope-mimetic membrane so as to better understand the proton conduction mechanism. In the high-pH closed state, the four histidines form an edge-face ?-stacked structure, preventing the formation of a hydrogen-bonded water chain to conduct protons. In the low-pH conducting state, the imidazoliums hydrogen-bond extensively with water and undergo microsecond ring reorientations with an energy barrier greater than 59 kilojoules per mole. This barrier is consistent with the temperature dependence of proton conductivity, suggesting that histidine-37 dynamically shuttles protons into the virion. We propose a proton conduction mechanism in which ring-flip-assisted imidazole deprotonation is the rate-limiting step.
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
Fanghao Hu, Klaus Schmidt-Rohr and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2081185/aop/images/medium/ja-2011-081185_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2081185
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/C3pPoB5_PR8
nmrlearner
Journal club
0
10-22-2011 10:16 AM
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Angew Chem Int Ed Engl. 2011 Apr 20;
Authors: Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez Del Amo JM, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B
nmrlearner
Journal club
0
04-22-2011 02:00 PM
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Proton-Detected Solid-State NMR Spectroscopy of Fibrillar and Membrane Proteins.
Angew Chem Int Ed Engl. 2011 Apr 14;
Authors: Linser R, Dasari M, Hiller M, Higman V, Fink U, Lopez Del Amo JM, Markovic S, Handel L, Kessler B, Schmieder P, Oesterhelt D, Oschkinat H, Reif B
nmrlearner
Journal club
0
04-16-2011 12:29 PM
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
A Proton-Detected 4D Solid-State NMR Experiment for Protein Structure Determination.
Chemphyschem. 2011 Apr 4;12(5):915-8
Authors: Huber M, Hiller S, Schanda P, Ernst M, Böckmann A, Verel R, Meier BH
nmrlearner
Journal club
0
03-29-2011 07:04 PM
[NMR paper] Expression and initial structural insights from solid-state NMR of the M2 proton chan
Expression and initial structural insights from solid-state NMR of the M2 proton channel from influenza A virus.
Related Articles Expression and initial structural insights from solid-state NMR of the M2 proton channel from influenza A virus.
Biochemistry. 2002 Sep 17;41(37):11294-300
Authors: Tian C, Tobler K, Lamb RA, Pinto LH, Cross TA
The M2 protein from influenza A virus has been expressed, purified, and reconstituted into DMPC/DMPG liposomes. SDS-PAGE analysis of reconstituted M2 protein in DMPC/DMPG liposomes demonstrates a stable...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] Direct refinement against proton-proton dipolar couplings in NMR structure determinat
Direct refinement against proton-proton dipolar couplings in NMR structure determination of macromolecules.
Related Articles Direct refinement against proton-proton dipolar couplings in NMR structure determination of macromolecules.
J Magn Reson. 2000 Feb;142(2):393-6
Authors: Tjandra N, Marquardt J, Clore GM
The computational tools necessary for making use of (1)H-(1)H dipolar couplings in macromolecular structure refinement are presented. Potentials are described for direct refinement against (1)H-(1)H dipolar couplings of known sign as well...
nmrlearner
Journal club
0
11-18-2010 09:15 PM
[NMR paper] Conformational changes of bacteriorhodopsin along the proton-conduction chain as stud
Conformational changes of bacteriorhodopsin along the proton-conduction chain as studied with (13)C NMR of Ala-labeled protein: arg(82) may function as an information mediator.
Related Articles Conformational changes of bacteriorhodopsin along the proton-conduction chain as studied with (13)C NMR of Ala-labeled protein: arg(82) may function as an information mediator.
Biophys J. 1999 Sep;77(3):1577-84
Authors: Tanio M, Tuzi S, Yamaguchi S, Kawaminami R, Naito A, Needleman R, Lanyi JK, Saitô H
We have recorded (13)C NMR spectra of Ala-labeled...