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Title: Oligomeric Structure of Anabaena Sensory Rhodopsin in a Lipid Bilayer Environment by Combining Solid-State NMR and Long-range DEER Constraints

Authors:
; ORCiD logo; ; ; ; ; ; ; ORCiD logo; ORCiD logo
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1415317
Grant/Contract Number:
FG02-02ER15354
Resource Type:
Journal Article: Publisher's Accepted Manuscript
Journal Name:
Journal of Molecular Biology
Additional Journal Information:
Journal Volume: 429; Journal Issue: 12; Related Information: CHORUS Timestamp: 2018-01-02 08:40:06; Journal ID: ISSN 0022-2836
Publisher:
Elsevier
Country of Publication:
United Kingdom
Language:
English

Citation Formats

Milikisiyants, Sergey, Wang, Shenlin, Munro, Rachel A., Donohue, Matthew, Ward, Meaghan E., Bolton, David, Brown, Leonid S., Smirnova, Tatyana I., Ladizhansky, Vladimir, and Smirnov, Alex I. Oligomeric Structure of Anabaena Sensory Rhodopsin in a Lipid Bilayer Environment by Combining Solid-State NMR and Long-range DEER Constraints. United Kingdom: N. p., 2017. Web. doi:10.1016/j.jmb.2017.05.005.
Milikisiyants, Sergey, Wang, Shenlin, Munro, Rachel A., Donohue, Matthew, Ward, Meaghan E., Bolton, David, Brown, Leonid S., Smirnova, Tatyana I., Ladizhansky, Vladimir, & Smirnov, Alex I. Oligomeric Structure of Anabaena Sensory Rhodopsin in a Lipid Bilayer Environment by Combining Solid-State NMR and Long-range DEER Constraints. United Kingdom. doi:10.1016/j.jmb.2017.05.005.
Milikisiyants, Sergey, Wang, Shenlin, Munro, Rachel A., Donohue, Matthew, Ward, Meaghan E., Bolton, David, Brown, Leonid S., Smirnova, Tatyana I., Ladizhansky, Vladimir, and Smirnov, Alex I. Thu . "Oligomeric Structure of Anabaena Sensory Rhodopsin in a Lipid Bilayer Environment by Combining Solid-State NMR and Long-range DEER Constraints". United Kingdom. doi:10.1016/j.jmb.2017.05.005.
@article{osti_1415317,
title = {Oligomeric Structure of Anabaena Sensory Rhodopsin in a Lipid Bilayer Environment by Combining Solid-State NMR and Long-range DEER Constraints},
author = {Milikisiyants, Sergey and Wang, Shenlin and Munro, Rachel A. and Donohue, Matthew and Ward, Meaghan E. and Bolton, David and Brown, Leonid S. and Smirnova, Tatyana I. and Ladizhansky, Vladimir and Smirnov, Alex I.},
abstractNote = {},
doi = {10.1016/j.jmb.2017.05.005},
journal = {Journal of Molecular Biology},
number = 12,
volume = 429,
place = {United Kingdom},
year = {Thu Jun 01 00:00:00 EDT 2017},
month = {Thu Jun 01 00:00:00 EDT 2017}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1016/j.jmb.2017.05.005

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  • Highly oriented samples of lipid and gramicidin A' (8:1 molar ratio) have been prepared with the samples extensively hydrated (approximately 70% water v/w). These preparations have been shown to be completely in a bilayer phase with a transition temperature of 28/sup 0/C, and evidence is presented indicating that the gramicidin is in the channel conformation. An estimate of the disorder in the alignment of the bilayers parallel with the glass plates used to align the bilayers can be made from the asymmetry of the nuclear magnetic resonances (NMR). Such an analysis indicates a maximal range of disorder of +-3/sup 0/.more » Uniformly /sup 15/N-labeled gramicidin has been biosynthesized by Bacillus brevis grown in a media containing /sup 15/N-labeled Escherichia coli cells as the only nitrogen source. When prepared with labeled gramicidin, the oriented samples result in high-resolution /sup 15/N NMR spectra showing 12 resonances for the 20 nitrogen sites of the polypeptide. The frequency of the three major multiple resonance peaks has been interpreted to yield the approximate orientation of the N-H bonds in the peptide linkages with respect to the magnetic field. The bond orientations are only partially consistent with the extant structural models of gramicidin.« less
  • Crystals of Anabaena sensory rhodopsin transducer, the transducer for the cyanobacterial photosensor Anabaena sensory rhodopsin, obtained in the space groups P4, C2 and P2{sub 1}2{sub 1}2{sub 1} diffract to 1.8, 2.1 and 2.0 Å, respectively. Phases for these crystal forms were obtained by SIRAS phasing using an iodide quick-soak derivative (P4) and molecular replacement (C2 and P2{sub 1}2{sub 1}2{sub 1}). Anabaena sensory rhodopsin transducer (ASRT) is a 14.7 kDa soluble signaling protein associated with the membrane-embedded light receptor Anabaena sensory rhodopsin (ASR) from Anabaena sp., a freshwater cyanobacterium. Crystals of ASRT were obtained in three different space groups, P4, C2more » and P2{sub 1}2{sub 1}2{sub 1}, which diffract to 1.8, 2.1 and 2.0 Å, respectively. Phases for one of these crystal forms (P4) were obtained by SIRAS phasing using an iodide quick-soak derivative and a partial model was built. Phases for the remaining crystal forms were obtained by molecular replacement using the partial model from the P4 crystal form.« less
  • Here, we report that spatial (<1 nm) proximity between different molecules in solid bulk materials and, for the first time, different moieties on the surface of a catalyst, can be established without isotope enrichment by means of homonuclear CHHC solid-state nuclear magnetic resonance experiment. This 13C– 13C correlation measurement, which hitherto was not possible for natural-abundance solids, was enabled by the use of dynamic nuclear polarization. Importantly, it allows the study of long-range correlations in a variety of materials with high resolution.
  • The opportunistic pathogen Pseudomonas aeruginosa may cause both acute and chronic-persistent infections in predisposed individuals. Acute infections require the presence of a functional type III secretion system (T3SS), whereas chronic P. aeruginosa infections are characterized by the formation of drug-resistant biofilms. The T3SS and biofilm formation are reciprocally regulated by the signaling kinases LadS, RetS, and GacS. RetS downregulates biofilm formation and upregulates expression of the T3SS through a unique mechanism. RetS forms a heterodimeric complex with GacS and thus prevents GacS autophosphorylation and downstream signaling. The signals that regulate RetS are not known but RetS possesses a distinctive periplasmicmore » sensor domain that is believed to serve as receptor for the regulatory ligand. We have determined the crystal structure of the RetS sensory domain at 2.0 {angstrom} resolution. The structure closely resembles those of carbohydrate binding modules of other proteins, suggesting that the elusive ligands are likely carbohydrate moieties. In addition to the conserved beta-sandwich structure, the sensory domain features two alpha helices which create a unique surface topology. Protein-protein crosslinking and fluorescence energy transfer experiments also revealed that the sensory domain dimerizes with a dissociation constant of K{sub d} = 580 {+-} 50 nM, a result with interesting implications for our understanding of the underlying signaling mechanism.« less