Structure of YF1. a Structure of YF1 in its dark-adapted state as

Download scientific diagram | Structure of YF1. a Structure of YF1 in its dark-adapted state as resolved by X-ray crystallography 13. The location of the different domains, of the flavin mononucleotide (FMN), of the cofactor adenosine diphosphate (ADP), and of the phosphoaccepting histidine 161 are indicated. b Light induced conformational changes of the LOV photosensor domain refined from X-ray solution scattering 22. The changes are maximal at the C-termini that feed into the Jα helices (dashed arrows). The coloring is according to the root mean square deviation of the alpha carbons  from publication: Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase | Sensor histidine kinases are central to sensing in bacteria and in plants. They usually contain sensor, linker, and kinase modules and the structure of many of these components is known. However, it is unclear how the kinase module is structurally regulated. Here, we use | Secondary Protein Structure, Bacterial Proteins and Protein Conformation | ResearchGate, the professional network for scientists.

Plant phytochrome B is an asymmetric dimer with unique signalling potential

Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1

PDF) Structure of theBacillus subtilisPhage SPO1-Encoded Type II DNA-binding Protein TF1 in Solution

PDF) Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase

Structure of the YtvA STAS (a) and LOV (b) domains with the position of

IJMS, Free Full-Text

Light-Oxygen-Voltage (LOV)-sensing Domains: Activation Mechanism and Optogenetic Stimulation - ScienceDirect

Ashley J. Hughes's research works University of Gothenburg, Göteborg (GU) and other places

Structural photoactivation of YF1. Blue light causes sequential

A structural model for the full-length blue light-sensing protein YtvA from Bacillus subtilis , based on EPR spectroscopy - Photochemical & Photobiological Sciences (RSC Publishing) DOI:10.1039/C3PP50128K