Structure of YF1. a Structure of YF1 in its dark-adapted state as
![](https://www.researchgate.net/publication/319175728/figure/fig1/AS:528751613812736@1503075616919/Structure-of-YF1-a-Structure-of-YF1-in-its-dark-adapted-state-as-resolved-by-X-ray_Q320.jpg)
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.
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Residue alterations within a conserved hydrophobic pocket influence light, oxygen, voltage photoreceptor dark recovery
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The six steps of the complete F1-ATPase rotary catalytic cycle
![](https://www.researchgate.net/publication/308761334/figure/fig4/AS:412056206495751@1475253263379/Structures-of-theaflavins-a-TF1-b-TF2B-c-TF2A-d-TF3.png)
Structures of theaflavins. a TF1, b TF2B, c TF2A, d TF3
![](https://www.researchgate.net/publication/46281185/figure/fig3/AS:386514551885826@1469163659035/Structural-changes-observed-in-the-F-1-structure-with-mgi-mutation-Val279Phe-A-and-B.png)
Structural changes observed in the F 1 structure with mgi mutation
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IJMS, Free Full-Text
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Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase
![](https://www.researchgate.net/publication/321811247/figure/fig4/AS:958806402031638@1605608668969/Conformations-of-the-macrocyclic-ring-hydrogen-bonded-to-the-initial-and-final-station_Q320.jpg)
Matthijs PANMAN, Scientist, PhD, VSL - Dutch Metrology Institute, Delft, VSL, Temperature and Humidity
![](https://www.researchgate.net/publication/360545470/figure/fig4/AS:1155102534574080@1652409313156/Light-response-of-AsLOV2-variants-a-Far-UV-circular-dichroism-CD-spectra-of-AsLOV2-in_Q320.jpg)
Ralph DIENSTHUBER, Dr., Humboldt-Universität zu Berlin, Berlin, HU Berlin, Department of Biology
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Structure of YF1. a Structure of YF1 in its dark-adapted state as
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Light-Oxygen-Voltage (LOV)-sensing Domains: Activation Mechanism and Optogenetic Stimulation - ScienceDirect
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Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an autoinhibited conformation
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PDF) Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase
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Structure of YF1. a Structure of YF1 in its dark-adapted state as