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Introduction: Playing football (American soccer) at the elite level places extremely high demands on the spine. The choice of treatment for lumbar spinal canal stenosis combined with spondylolysis and anterolisthesis is challenging for surgeons, physicians, and clinicians. Case Presentation: A 28-year-old elite football player from the leading Russian football club is the focus of this case study. Patient complained of constant low back pain radiating to the posterior surface of the right thigh and limited mobility in the lumbar spine. Diagnosis: The patient was diagnosed with degenerative stenosis of the spinal canal at the L5 to S1 level, L4 to L5 disc herniation, spondylolysis, and anterolisthesis of L5 vertebra. Management and Outcomes: Two-stage surgery of combined lumbar spine pathology was performed in May 2021. The first stage of surgical treatment included the spinal and foraminal canals decompression at the L4 to L5 and L5 to S1 levels, as well as posterior fusion with rigid pedicle screws. The second stage involved the subsequent replacement of the rigid to dynamic semirigid rods as signs of the bone defect healing appeared. The athlete returned to team training 6 months after the first stage of surgery and was able to play football at the elite level without restrictions 1 year after the first stage and just 30 days following the second stage of surgical treatment. The athlete continues his career as of the last manuscript's revision. Conclusions: This method holds potential as an effective approach in the treatment of combined lumbar spine pathology among elite athletes. [ABSTRACT FROM AUTHOR]

The Dps protein is the major DNA-binding protein of prokaryotes, which protects DNA during starvation by forming a crystalline complex. The structure of such an intracellular DNA-Dps complex is still unknown. However, the phenomenon of a decrease in the size of the Dps protein from 90 Å to 69–75 Å during the formation of a complex with DNA has been repeatedly observed, and no explanation has been given. In this work, we show that during the formation of intracellular DNA–Dps crystals, the protein transitions to another oligomeric form: from a dodecameric (of 12 monomers), which has an almost spherical shape with a diameter of 90 Å, to a trimeric (of three monomers), which has a shape close to a torus-like structure with a diameter of 70 Å and a height of 40 Å. The trimer model was obtained through the molecular dynamic modeling of the interaction of the three monomers of the Dps protein. Placement of the obtained trimer in the electron density of in vitro DNA–Dps crystal allowed for the determination of the lattice parameters of the studied crystal. This crystal model was in good agreement with the SAXS data obtained from intracellular crystals of 2-day-old Escherichia coli cells. The final crystal structure contains a DNA molecule in the through channel of the crystal structure between the Dps trimers. It was discussed that the mechanism of protein transition from one oligomeric form to another in the cell cytoplasm could be regulated by intracellular metabolites and is a simple and flexible mechanism of prokaryotic cell transition from one metabolic state to another. [ABSTRACT FROM AUTHOR]