[NMR paper] Oligomeric Structure of Anabaena Sensory Rhodopsin in a Lipid Bilayer Environment by Combining Solid-State NMR and Long-range DEER Constraints.
Related ArticlesOligomeric Structure of Anabaena Sensory Rhodopsin in a Lipid Bilayer Environment by Combining Solid-State NMR and Long-range DEER Constraints.
J Mol Biol. 2017 May 10;:
Authors: Milikisiyants S, Wang S, Munro RA, Donohue M, Ward ME, Bolton D, Brown LS, Smirnova TI, Ladizhansky V, Smirnov AI
Abstract
Oligomerization of membrane proteins is common in nature. Here, we combine spin-labeling Double Electron-Electron Resonance (DEER) and solid-state NMR (ssNMR) spectroscopy to refine the structure of an oligomeric integral membrane protein, Anabaena Sensory Rhodopsin (ASR), reconstituted in a lipid environment. An essential feature of such a combined approach is that it provides structural distance restraints spanning a range of ca. 3-60Å, while using the same sample preparation (i.e., mutations, paramagnetic labeling, and reconstitution in lipid bilayers) for both ssNMR and DEER. Direct modelling of the multispin effects on DEER signal allowed for the determination of the oligomeric order and for obtaining long-range DEER distance restraints between the ASR trimer subunits that were used to refine solid-state NMR structure of ASR. The improved structure of the ASR trimer revealed a more compact packing of helices and side chains at the intermonomer interface, compared to the structure determined using the ssNMR data alone. The extent of the refinement is significant when compared with typical helix movements observed for the active states of homologous proteins. Our combined approach of using complementary DEER and NMR measurements for the determination of oligomeric structures would be widely applicable to membrane proteins where paramagnetic tags can be introduced. Such a method could be used to study the effects of the lipid membrane composition on protein oligomerization as well as to observe structural changes in protein oligomers upon drug, substrate, and co-factor binding.
PMID: 28501588 [PubMed - as supplied by publisher]
[NMR paper] Color-discriminating retinal configurations of sensory rhodopsin I by photo-irradiation solid-state NMR spectroscopy.
Color-discriminating retinal configurations of sensory rhodopsin I by photo-irradiation solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary_FullTextOnline_120x27.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary_FullTextOnline_120x27.gif Related Articles Color-discriminating retinal configurations of sensory rhodopsin I by photo-irradiation solid-state NMR spectroscopy.
Angew Chem Int Ed...
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[NMR paper] Advanced solid-state NMR techniques for characterization of membrane protein structure and dynamics: Application to Anabaena Sensory Rhodopsin.
Advanced solid-state NMR techniques for characterization of membrane protein structure and dynamics: Application to Anabaena Sensory Rhodopsin.
Related Articles Advanced solid-state NMR techniques for characterization of membrane protein structure and dynamics: Application to Anabaena Sensory Rhodopsin.
J Magn Reson. 2014 Dec 26;
Authors: Ward ME, Brown LS, Ladizhansky V
Abstract
Studies of the structure, dynamics, and function of membrane proteins (MPs) have long been considered one of the main applications of solid-state...
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[NMR paper] Advanced Solid-State NMR Techniques for Characterization of Membrane Protein Structure and Dynamics: Application to Anabaena Sensory Rhodopsin
Advanced Solid-State NMR Techniques for Characterization of Membrane Protein Structure and Dynamics: Application to Anabaena Sensory Rhodopsin
Publication date: Available online 26 December 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Meaghan E. Ward , Leonid S. Brown , Vladimir Ladizhansky</br>
Studies of the structure, dynamics, and function of membrane proteins (MPs) have long been considered one of the main applications of solid-state NMR (SSNMR). Advances in instrumentation, and the plethora of new SSNMR methodologies developed over the past...
ConformationalDynamics of a Seven Transmembrane HelicalProtein Anabaena Sensory RhodopsinProbed by Solid-State NMR
ConformationalDynamics of a Seven Transmembrane HelicalProtein Anabaena Sensory RhodopsinProbed by Solid-State NMR
Daryl B. Good, Shenlin Wang, Meaghan E. Ward, Jochem Struppe, Leonid S. Brown, Jo?zef R. Lewandowski and Vladimir Ladizhansky
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja411633w/aop/images/medium/ja-2013-11633w_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja411633w
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http://feeds.feedburner.com/~r/acs/jacsat/~4/MTq1JhQmGFU
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[NMR paper] Conformational dynamics of a seven transmembrane helical protein Anabaena Sensory Rhodopsin probed by solid-state NMR.
Conformational dynamics of a seven transmembrane helical protein Anabaena Sensory Rhodopsin probed by solid-state NMR.
Related Articles Conformational dynamics of a seven transmembrane helical protein Anabaena Sensory Rhodopsin probed by solid-state NMR.
J Am Chem Soc. 2014 Jan 27;
Authors: Good DB, Wang S, Ward ME, Struppe JO, Brown LS, Lewandowski JR, Ladizhansky V
Abstract
The ability to detect and characterize molecular motions represents one of the unique strengths of Nuclear Magnetic Resonance (NMR) spectroscopy. In this study we...
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[NMR paper] Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Acc Chem Res. 2013 Jul 5;
Authors: Opella SJ
Abstract
One of the most important topics in experimental structural biology is determining the structures of membrane proteins. These structures represent one-third of all of the information...
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[NMR paper] Structure of gramicidin a in a lipid bilayer environment determined using molecular d
Structure of gramicidin a in a lipid bilayer environment determined using molecular dynamics simulations and solid-state NMR data.
Related Articles Structure of gramicidin a in a lipid bilayer environment determined using molecular dynamics simulations and solid-state NMR data.
J Am Chem Soc. 2003 Aug 13;125(32):9868-77
Authors: Allen TW, Andersen OS, Roux B
Two different high-resolution structures recently have been proposed for the membrane-spanning gramicidin A channel: one based on solid-state NMR experiments in oriented phospholipid...
Oligomeric Structure of Anabaena Sensory Rhodopsin in a Lipid Bilayer Environment by Combining Solid-State NMR and Long-range DEER Constraints.
Linear Mode
