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8A7H

Crystal structure of a chimeric LOV-Histidine kinase SB2F1-I66R mutant (light state; asymmetrical variant, trigonal form with long c axis)

Summary for 8A7H
Entry DOI10.2210/pdb8a7h/pdb
DescriptorPutative Sensory box protein,Sensor protein FixL, ADENOSINE-5'-TRIPHOSPHATE, Flavin mononucleotide (semi-quinone intermediate) (3 entities in total)
Functional Keywordslov domain, pas domain, photocycle, dimerization, signaling blue light photoreceptor, sensory histidine kinase, chimeric, de novo protein, signaling protein
Biological sourcePseudomonas putida KT2440
More
Total number of polymer chains2
Total formula weight87819.14
Authors
Arinkin, V.,Granzin, J.,Batra-Safferling, R. (deposition date: 2022-06-21, release date: 2024-01-10, Last modification date: 2026-07-15)
Primary citationArinkin, V.,Stadler, A.M.,Meier, S.S.M.,Jaeger, K.E.,Moglich, A.,Krauss, U.,Batra-Safferling, R.
Dimer asymmetry in signaling of blue light sensor histidine kinases.
Sci Adv, 12:eaed8943-eaed8943, 2026
Cited by
PubMed Abstract: Photoreceptor sensory histidine kinases (SHKs) couple light absorption to conformational changes regulating two-component signaling. Despite their importance and widespread use in optogenetics, the underlying structural signaling mechanisms remain poorly understood. Here, we engineered dimeric SHKs based on short light-oxygen-voltage (LOV) proteins, determined their crystal structures, and investigated their signaling mechanisms. Regardless of illumination, the structures adopted a light-state like LOV-LOV dimer with symmetric/straight kinase modules. In contrast, small-angle x-ray scattering together with functional assays revealed pronounced light-dependent rearrangements in solution and allowed the assignment of the kinase-ON dark state to an asymmetric/kinked conformation, whereas the light state adopts a symmetric/straight structure. Comparative analyses of natural and engineered SHKs identified conserved motifs linking light-induced LOV domain rotation to kinase activity. The findings highlight the central role of dimer asymmetry and flexibility in SHK signaling, thereby not least informing the engineering of new light-responsive signaling systems.
PubMed: 42384803
DOI: 10.1126/sciadv.aed8943
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.145 Å)
Structure validation

257629

건을2026-08-05부터공개중

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