8A6X
Crystal structure of a chimeric LOV-Histidine kinase SB2F1 (asymmetrical variant, trigonal form with long c axis)
Summary for 8A6X
| Entry DOI | 10.2210/pdb8a6x/pdb |
| Descriptor | Putative Sensory box protein,Sensor protein FixL, ADENOSINE-5'-TRIPHOSPHATE, FLAVIN MONONUCLEOTIDE (3 entities in total) |
| Functional Keywords | lov domain; pas domain; photocycle; dimerization; signaling blue light photoreceptor; sensory histidine kinase; chimeric; de novo protein, signaling protein |
| Biological source | Pseudomonas putida KT2440 More |
| Total number of polymer chains | 2 |
| Total formula weight | 88664.93 |
| Authors | Arinkin, V.,Granzin, J.,Batra-Safferling, R. (deposition date: 2022-06-20, release date: 2024-01-10, Last modification date: 2026-07-15) |
| Primary citation | Arinkin, 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: 42384803DOI: 10.1126/sciadv.aed8943 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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