Phytochromes perceive subtle changes in the light environment and convert them into biological signals by photoconversion between the red-light absorbing (Pr) and the far-red-absorbing (Pfr) states. In the primitive bacteriophytochromes this includes refolding of a tongue-like hairpin loop close to the chromophore, one strand of an antiparallel b-sheet being replaced by ?-helix. However, the strand sequence in the cyanobacterial phytochrome Cph1 is different from that of previously investigated...
Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation
Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation
Abstract
Biofilms are accumulations of microorganisms embedded in extracellular matrices that protect against external factors and stressful environments. Cyanobacterial biofilms are ubiquitous and have potential for treatment of wastewater and sustainable production of biofuels. But the underlying mechanisms regulating cyanobacterial biofilm formation are unclear. Here, we report the solution NMR structure of a protein, Se0862, conserved across diverse cyanobacterial species and...
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10-25-2020 01:39 PM
Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation
Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation
ABSTRACT
Biofilms are accumulations of microorganisms embedded in extracellular matrices that protect against external factors and stressful environments. Cyanobacterial biofilms are ubiquitous and have potential for treatment of wastewater and sustainable production of biofuels. But the underlying mechanisms regulating cyanobacterial biofilm formation are unclear. Here, we report the solution NMR structure of a protein, Se0862, conserved across diverse cyanobacterial species and...
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09-21-2020 05:44 PM
[NMR paper] Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation.
Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7388-69-wiley-full-text.png Related Articles Solution NMR structure of Se0862, a highly conserved cyanobacterial protein involved in biofilm formation.
Protein Sci. 2020 Sep 18;:
Authors: Zhang N, Chang YG, Tseng R, Ovchinnikov S, Schwarz R, LiWang A
Abstract
Biofilms are accumulations of microorganisms embedded in...
[NMR paper] 3D Structures of Plant Phytochrome A as Pr and Pfr From Solid-State NMR: Implications for Molecular Function.
3D Structures of Plant Phytochrome A as Pr and Pfr From Solid-State NMR: Implications for Molecular Function.
Related Articles 3D Structures of Plant Phytochrome A as Pr and Pfr From Solid-State NMR: Implications for Molecular Function.
Front Plant Sci. 2018;9:498
Authors: Song C, Mroginski MA, Lang C, Kopycki J, Gärtner W, Matysik J, Hughes J
Abstract
We present structural information for oat phyA3 in the far-red-light-absorbing (Pfr) signaling state, to our knowledge the first three-dimensional (3D) information for a plant...
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05-10-2018 01:31 PM
[NMR paper] NMR chemical shift pattern changed by ammonium sulfate precipitation in cyanobacterial phytochrome Cph1.
NMR chemical shift pattern changed by ammonium sulfate precipitation in cyanobacterial phytochrome Cph1.
Related Articles NMR chemical shift pattern changed by ammonium sulfate precipitation in cyanobacterial phytochrome Cph1.
Front Mol Biosci. 2015;2:42
Authors: Song C, Lang C, Kopycki J, Hughes J, Matysik J
Abstract
Phytochromes are dimeric biliprotein photoreceptors exhibiting characteristic red/far-red photocycles. Full-length cyanobacterial phytochrome Cph1 from Synechocystis 6803 is soluble initially but tends to aggregate...
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08-19-2015 03:24 PM
[NMR paper] CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts.
CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts.
Related Articles CSI 3.0: a web server for identifying secondary and super-secondary structure in proteins using NMR chemical shifts.
Nucleic Acids Res. 2015 May 15;
Authors: Hafsa NE, Arndt D, Wishart DS
Abstract
The Chemical Shift Index or CSI 3.0 (http://csi3.wishartlab.com) is a web server designed to accurately identify the location of secondary and super-secondary structures in protein chains using only...
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05-17-2015 03:52 PM
Crystal structure of a cyanobacterial protein associated with nitrogen fixation - Phys.Org
Crystal structure of a cyanobacterial protein associated with nitrogen fixation - Phys.Org
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Crystal structure of a cyanobacterial protein associated with nitrogen fixation
Phys.Org
NMR and other biophysical data collected at EMSL confirmed that the biological unit of DUF269 in solution was the same as observed in the asymmetric unit of the crystal, a dimer. Further biochemical experiments are in progress to determine the ...
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Changes in Secondary Structure upon Pr to Pfr Transition in Cyanobacterial Phytochrome Cph1 detected by DNP NMR
Linear Mode
