Publication date: Available online 9 June 2016 Source:Journal of Molecular Biology
Author(s): Katrin Röllen, Joachim Granzin, Vineet Panwalkar, Vladimir Arinkin, Raj Rani, Rudolf Hartmann, Ulrich Krauss, Karl-Erich Jaeger, Dieter Willbold, Renu Batra-Safferling
LOV (Light-Oxygen-Voltage) domains represent the photo-responsive domains of various blue-light photoreceptor proteins and are widely distributed in plants, algae, fungi and bacteria. Here, we report the dark state crystal structure of PpSB1-LOV, a slow-reverting short LOV protein from Pseudomonas putida which is remarkably different from our previously published ‘fully light-adapted’ structure [1]. A direct comparison of the two structures provides insight into the light-activated signaling mechanism. Major structural differences involve a~11Å movement of the C-terminus in helix J?, ~4Å movement of H?-I? loop, disruption of hydrogen bonds in the dimer interface, and a~29 ° rotation of chain-B relative to chain-A as compared to the light state dimer. Both, crystal structures and solution NMR data are suggestive of the key roles of a conserved glutamine Q116 and the N-cap region consisting of A'?-A? loop and the A'? helix in controlling the light-activated conformational changes. The activation mechanism proposed here for the PpSB1-LOV supports a rotary switch mechanism and provides insights into the signal propagation mechanism in naturally existing and artificial LOV-based two-component systems and regulators. Graphical abstract
Photochemical Reactions of the LOV and LOV-LinkerDomains of the Blue Light Sensor Protein YtvA
Photochemical Reactions of the LOV and LOV-LinkerDomains of the Blue Light Sensor Protein YtvA
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00263/20160527/images/medium/bi-2016-00263j_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00263
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/or4L4jAycnA
More...
nmrlearner
Journal club
0
05-28-2016 01:48 PM
[NMR paper] Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures.
Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures.
Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures.
J Am Chem Soc. 2014 Jan 6;
Authors: Mao B, Tejero R, Baker D, Montelione GT
Abstract
We have found that refinement of protein NMR structures using Rosetta with experimental NMR restraints yields more accurate protein NMR structures than those that have been deposited in the PDB using standard refinement...
nmrlearner
Journal club
0
01-08-2014 11:23 AM
[NMR paper] Intrinsic Allosteric Inhibition of Signaling Proteins by Targeting Rare Interaction States Detected by High-Pressure NMR Spectroscopy.
Intrinsic Allosteric Inhibition of Signaling Proteins by Targeting Rare Interaction States Detected by High-Pressure NMR Spectroscopy.
Related Articles Intrinsic Allosteric Inhibition of Signaling Proteins by Targeting Rare Interaction States Detected by High-Pressure NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Nov 11;
Authors: Kalbitzer HR, Rosnizeck IC, Munte CE, Narayanan SP, Kropf V, Spoerner M
Abstract
A new type of allosteric inhibition by small molecules is proposed that should be applicable to all proteins involved intrinsically...
nmrlearner
Journal club
0
11-13-2013 09:22 PM
[NMR paper] An NMR comparison of the light-harvesting complex II (LHCII) in active and photoprotective states reveals subtle changes in the chlorophyll a ground-state electronic structures.
An NMR comparison of the light-harvesting complex II (LHCII) in active and photoprotective states reveals subtle changes in the chlorophyll a ground-state electronic structures.
Related Articles An NMR comparison of the light-harvesting complex II (LHCII) in active and photoprotective states reveals subtle changes in the chlorophyll a ground-state electronic structures.
Biochim Biophys Acta. 2013 Mar 4;
Authors: Pandit A, Reus M, Morosinotto T, Bassi R, Holzwarth AR, de Groot HJ
Abstract
To protect the photosynthetic apparatus against...
nmrlearner
Journal club
0
03-08-2013 10:35 PM
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy [Biophysics and Computational Biology]
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy
Masterson, L. R., Shi, L., Metcalfe, E., Gao, J., Taylor, S. S., Veglia, G....
Date: 2011-04-26
Protein kinase A (PKA) is a ubiquitous phosphoryl transferase that mediates hundreds of cell signaling events. During turnover, its catalytic subunit (PKA-C) interconverts between three major conformational states (open, intermediate, and closed) that are dynamically and allosterically activated by nucleotide binding. We show that the structural transitions between these...
nmrlearner
Journal club
0
04-27-2011 04:16 AM
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.
Proc Natl Acad Sci U S A. 2011 Apr 6;
Authors: Masterson LR, Shi L, Metcalfe E, Gao J, Taylor SS, Veglia G
Protein kinase A (PKA) is a ubiquitous phosphoryl transferase that mediates hundreds of cell signaling events. During turnover, its catalytic subunit (PKA-C) interconverts between three major conformational states...
nmrlearner
Journal club
0
04-08-2011 10:00 AM
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
J Struct Funct Genomics. 2010 Dec 14;
Authors: Mani R, Vorobiev S, Swapna GV, Neely H, Janjua H, Ciccosanti C, Xiao R, Acton TB, Everett JK, Hunt J, Montelione GT
The conserved Lipoprotein-17 domain of membrane-associated protein Q9PRA0_UREPA from Ureaplasma parvum was selected for structure determination by the Northeast Structural...
nmrlearner
Journal club
0
12-15-2010 12:03 PM
[NMR paper] Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures
Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us.
Related Articles Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us.
Prog Lipid Res. 2004 May;43(3):177-99
Authors: Hamilton JA
The interactions of fatty acids with proteins have been studied by a variety of conventional approaches for decades. However, only limited aspects of fatty acid-protein interactions have been elucidated, even with the integration of information gleaned from the many techniques....
Signaling states of a short blue light photoreceptor protein PpSB1-LOV revealed from crystal structures and solution NMR spectroscopy
Linear Mode
