High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution - Wikidata - awgldk - TriplyDB

High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution

High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution

http://www.wikidata.org/entity/Q27643899

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Phytochromes: an atomic perspective on photoactivation and signaling Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion Solution Structure of a Cyanobacterial Phytochrome GAF Domain in the Red-Light-Absorbing Ground State The structure of a complete phytochrome sensory module in the Pr ground state Crystal structure of Pseudomonas aeruginosa bacteriophytochrome: Photoconversion and signal transduction 2.3 A X-ray structure of the heme-bound GAF domain of sensory histidine kinase DosT of Mycobacterium tuberculosis Structural basis for the photoconversion of a phytochrome to the activated Pfr form Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome Structures of cyanobacteriochromes from phototaxis regulators AnPixJ and TePixJ reveal general and specific photoconversion mechanism Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein Signal amplification and transduction in phytochrome photosensors Crystal structure of the photosensing module from a red/far-red light-absorbing plant phytochrome Crystallographic and Electron Microscopic Analyses of a Bacterial Phytochrome Reveal Local and Global Rearrangements during Photoconversion X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. radiodurans phytochrome Light signal transduction: an infinite spectrum of possibilities Tolerance of a Knotted Near-Infrared Fluorescent Protein to Random Circular Permutation Folding analysis of the most complex Stevedore's protein knot Perception of the plant hormone ethylene: known-knowns and known-unknowns The D-ring, not the A-ring, rotates in Synechococcus OS-B' phytochrome.Dynamic structural changes underpin photoconversion of a blue/green cyanobacteriochrome between its dark and photoactivated states.Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers A knot in the protein structure - probing the near-infrared fluorescent protein iRFP designed from a bacterial phytochrome.A second conserved GAF domain cysteine is required for the blue/green photoreversibility of cyanobacteriochrome Tlr0924 from Thermosynechococcus elongatus.Distinct classes of red/far-red photochemistry within the phytochrome superfamily.Light-induced chromophore activity and signal transduction in phytochromes observed by 13C and 15N magic-angle spinning NMR.Residues clustered in the light-sensing knot of phytochrome B are necessary for conformer-specific binding to signaling partner PIF3.Chromophore structure of cyanobacterial phytochrome Cph1 in the Pr state: reconciling structural and spectroscopic data by QM/MM calculations.Epitope mapping of monoclonal antibodies for the Deinococcus radiodurans bacteriophytochome.A brief history of phytochromes Proton-transfer and hydrogen-bond interactions determine fluorescence quantum yield and photochemical efficiency of bacteriophytochrome.Quaternary organization of a phytochrome dimer as revealed by cryoelectron microscopy FTIR Spectroscopy Revealing Light-Dependent Refolding of the Conserved Tongue Region of Bacteriophytochrome.Biliverdin amides reveal roles for propionate side chains in bilin reductase recognition and in holophytochrome assembly and photoconversion.Origins of fluorescence in evolved bacteriophytochromes Ultrafast red light activation of Synechocystis phytochrome Cph1 triggers major structural change to form the Pfr signalling-competent state.Two ground state isoforms and a chromophore D-ring photoflip triggering extensive intramolecular changes in a canonical phytochrome.Combining random gene fission and rational gene fusion to discover near-infrared fluorescent protein fragments that report on protein-protein interactions.Atomic force microscopy of red-light photoreceptors using peakforce quantitative nanomechanical property mapping.Characterization of two thermostable cyanobacterial phytochromes reveals global movements in the chromophore-binding domain during photoconversion.Light Signaling Mechanism of Two Tandem Bacteriophytochromes.

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High resolution structure of Deinococcus bacteriophytochrome yields new insights into phytochrome architecture and evolution

http://www.wikidata.org/entity/Q27643899

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2007 nî lūn-bûn

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2007 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2007 թվականի ապրիլին հրատարակված գիտական հոդված

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2007年の論文

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High resolution structure of D ...... ome architecture and evolution

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High resolution structure of D ...... ome architecture and evolution

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High resolution structure of D ...... ome architecture and evolution

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High resolution structure of D ...... ome architecture and evolution

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High resolution structure of D ...... ome architecture and evolution

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High resolution structure of D ...... ome architecture and evolution

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Jeremiah R Wagner

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Joseph S Brunzelle

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Junrui Zhang

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Katrina T Forest

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Richard D Vierstra

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P2860

The Protein Data Bank

Computational analysis and prediction of the binding motif and protein interacting partners of the Abl SH3 domain.

Processing of X-ray diffraction data collected in oscillation mode

Structure of a protein photocycle intermediate by millisecond time-resolved crystallography

Use of TLS parameters to model anisotropic displacements in macromolecular refinement

Coot: model-building tools for molecular graphics

Refinement of macromolecular structures by the maximum-likelihood method

XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

AMoRe: an automated package for molecular replacement

Expression, purification, and crystallization of the RGS-like domain from the Rho nucleotide exchange factor, PDZ-RhoGEF, using the surface entropy reduction approach.

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10.1074/JBC.M611824200

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16

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282

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