The influenza A M2 protein forms a proton channel for virus infection and mediates virus assembly and budding. While extensive structural information is known about the transmembrane helix and an adjacent amphipathic helix, the conformation of the N-terminal ectodomain and the C-terminal cytoplasmic tail remains largely unknown. Using two-dimensional (2D) magic-angle-spinning solid-state NMR, we have investigated the secondary structure and dynamics of full-length M2 (M2FL) and found them to depend on the membrane composition. In 2D 13C DARR correlation spectra, 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)-bound M2FL exhibits several peaks at ?-sheet chemical shifts, which result from water-exposed extramembrane residues. In contrast, M2FL bound to cholesterol-containing membranes gives predominantly ?-helical chemical shifts. Two-dimensional J-INADEQUATE spectra and variable-temperature 13C spectra indicate that DMPC-bound M2FL is highly dynamic while the cholesterol-containing membranes significantly immobilize the protein at physiological temperature. Chemical-shift prediction for various secondary-structure models suggests that the ?-strand is located at the N-terminus of the DMPC-bound protein, while the cytoplasmic domain is unstructured. This prediction is confirmed by the 2D DARR spectrum of the ectodomain-truncated M2(21–97), which no longer exhibits ?-sheet chemical shifts in the DMPC-bound state. We propose that the M2 conformational change results from the influence of cholesterol, and the increased helicity of M2FL in cholesterol-rich membranes may be relevant for M2 interaction with the matrix protein M1 during virus assembly and budding. The successful determination of the ?-strand location suggests that chemical-shift prediction is a promising approach for obtaining structural information of disordered proteins before resonance assignment.
[NMR paper] Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR.
Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR.
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 Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR.
Protein Sci. 2013 Sep 10;
Authors: Liao SY, Fritzsching KJ, Hong M
Abstract
The influenza A M2 protein forms a proton channel for virus infection and mediates virus...
nmrlearner
Journal club
0
09-12-2013 11:02 PM
Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR
Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR
Abstract
The influenza A M2 protein forms a proton channel for virus infection and mediates virus assembly and budding. While extensive structural information is known about the transmembrane (TM) helix and an adjacent amphipathic helix (AH), the conformation of the N-terminal ectodomain and the C-terminal cytoplasmic tail remains largely unknown. Using 2D magic-angle-spinning (MAS) solid-state NMR, we have investigated the secondary structure and dynamics of full-length M2 (M2FL) and...
nmrlearner
Journal club
0
09-10-2013 08:44 PM
[NMR paper] Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Dynamic Interaction Between Membrane-Bound Full-Length Cytochrome P450 and Cytochrome b5 Observed by Solid-State NMR Spectroscopy.
Sci Rep. 2013 Aug 29;3:2538
Authors: Yamamoto K, Dürr UH, Xu J, Im SC, Waskell L, Ramamoorthy A
Abstract
Microsomal monoxygenase enzymes of the cytochrome-P450 family are found in all biological kingdoms, and play a central role in the breakdown of metabolic as well as...
nmrlearner
Journal club
0
08-30-2013 04:35 PM
[NMR paper] Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p.
Biomol NMR Assign. 2013 Aug 14;
Authors: Schütz AK, Habenstein B, Luckgei N, Bousset L, Sourigues Y, Nielsen AB, Melki R, Böckmann A, Meier BH
Abstract
Sup35p is a yeast prion and is responsible for the trait in Saccharomyces cerevisiae. With 685 amino acids, full-length soluble and fibrillar Sup35p are challenging targets for structural biology as they cannot be investigated...
nmrlearner
Journal club
0
08-15-2013 07:45 PM
Drug-Induced Conformational and Dynamical Changes of the S31N Mutant of the Influenza M2 Proton Channel Investigated by Solid-State NMR
Drug-Induced Conformational and Dynamical Changes of the S31N Mutant of the Influenza M2 Proton Channel Investigated by Solid-State NMR
Jonathan K. Williams, Daniel Tietze, Jun Wang, Yibing Wu, William F. DeGrado and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja4041412/aop/images/medium/ja-2013-041412_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja4041412
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/SJt4vbTURaE
nmrlearner
Journal club
0
06-22-2013 01:40 AM
[NMR paper] Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.
Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.
Related Articles Protein oligomers studied by solid-state NMR: the case of full-length nucleoid associated protein H-NS.
FEBS J. 2013 Apr 20;
Authors: Renault M, García J, Cordeiro TN, Baldus M, Pons M
Abstract
Members of the histone-like nucleoid structuring protein (H-NS) family play roles both as architectural proteins and as modulators of gene expression in Gram-negative bacteria. The H-NS protein participates in modulatory processes...
nmrlearner
Journal club
0
04-23-2013 08:37 PM
[NMR paper] Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.
Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.
J Biomol NMR. 2013 Jan 18;
Authors: Ghosh U, Xie L, Weliky DP
Abstract...
nmrlearner
Journal club
0
02-03-2013 10:19 AM
[NMR paper] Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)
Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)N polarization inversion spin exchange at magic angle NMR.
Related Articles Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)N polarization inversion spin exchange at magic angle NMR.
Biophys J. 2000 Aug;79(2):767-75
Authors: Song Z, Kovacs FA, Wang J, Denny JK, Shekar SC, Quine JR, Cross TA
The M2 protein from the influenza A virus forms a proton channel in the virion that is essential for infection. This tetrameric protein...
Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR
Linear Mode
