Related ArticlesSolid-state NMR studies of full-length BamA in lipid bilayers suggest limited overall POTRA mobility.
J Mol Biol. 2014 Feb 12;
Authors: Sinnige T, Weingarth M, Renault M, Baker L, Tommassen J, Baldus M
Abstract
The outer membrane protein BamA is the key player in ?-barrel assembly in Gram-negative bacteria. Despite the availability of high-resolution crystal structures, the dynamic behavior of the transmembrane domain and the large periplasmic extension consisting of five POTRA domains remains unclear. We demonstrate reconstitution of full-length BamA in proteoliposomes at low lipid-to-protein ratio, leading to high sensitivity and resolution in solid-state NMR (ssNMR) experiments. We detect POTRA domains in ssNMR experiments probing rigid protein segments in our preparations. These results suggest that the periplasmic region of BamA is firmly attached to the ?-barrel and does not experience fast global motion around the angle between POTRA 2 and 3. We show that this behavior holds at lower protein concentrations and elevated temperatures. Chemical-shift variations observed after reconstitution in lipids with different chain lengths and saturation levels are compatible with conformational plasticity of BamA's transmembrane domain. Electron microscopy of the ssNMR samples shows that BamA can cause local disruptions of the lipid bilayer in proteoliposomes. The observed interplay between protein-protein and protein-lipid interactions may be critical for BamA-mediated insertion of substrates into the outer membrane.
PMID: 24530687 [PubMed - as supplied by publisher]
[NMR paper] Investigation of the mechanism of action of novel amphipathic peptides: Insights from solid-state NMR studies of oriented lipid bilayers.
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
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 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...
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10-07-2013 08:31 AM
[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...
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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...
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09-10-2013 08:44 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...
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08-15-2013 07:45 PM
[NMR paper] Full-length Vpu and human CD4(372-433) in phospholipid bilayers as seen by magic angle spinning NMR.
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Biol Chem. 2013 Jul 17;
Authors: Do HQ, Wittlich M, Glück JM, Möckel L, Willbold D, Koenig BW, Heise H
Abstract
Abstract HIV-1 Vpu and CD4(372-433), a peptide comprising the transmembrane and cytoplasmic domain of human CD4, were recombinantly expressed in Escherichia coli, uniformly labeled with 13C und 15N isotopes,...
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07-19-2013 09:20 PM
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
J Am Chem Soc. 2011 Mar 14;
Authors: Yang J, Aslimovska L, Glaubitz C
Environmental factors such as temperature, hydration, and lipid bilayer properties are tightly coupled to the dynamics of membrane proteins. So far, site-resolved data visualizing the protein's response to alterations in these factors are rare, and conclusions had to be drawn from dynamic data averaged over the whole protein...
Solid-state NMR studies of full-length BamA in lipid bilayers suggest limited overall POTRA mobility.
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