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<p>The orange carotenoid protein (OCP) plays a pivotal role in the photoprotection of cyanobacteria and undergoes a structural change after photoactivation. Here, we report a solution structure of the active state differing significantly from that known upon binding to the phycobilisome. In solution, the N-terminal domains are clearly detached and reoriented by about 90° relative to the C- terminal domains. This apparent structural difference implies the need for a previously unknown structural rearrangement. A rarely considered aspect is the internal protein dynamics facilitating this structural transition. Therefore, we directly probe protein dynamics in a wide observation time range in the dark and under illumination. After photoactivation to the active state, the internal dynamics is enhanced, while the global diffusion is slowed down. A residue-resolved molecular dynamics simulation indicates that the interdomain linker becomes more flexible and may mediate the structural adaptation to the phycobilisome binding site. In turn, the β-sheet structures remain the most rigid part of the active state structure, which is essential for protein dimerization.</p>

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Protein/linker dynamics facilitates the structural adaptation of the orange carotenoid protein in cyanobacterial photoprotection: a neutron scattering study

  • 期刊论文

  • 发表日期：

    2026年3月7日

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  • Maksym Golub,
  • Marcus Moldenhauer,
  • Franz-Josef Schmitt,
  • Tilo Seydel,
  • Markus Appel,
  • Olga Matsarskaia,
  • Sylvain Prevost,
  • Dmitry Zlenko,
  • Eugene G. Maksimov,
  • Roberta Spadaccini,
  • Thomas Friedrich,
  • Jörg Pieper

摘要

The orange carotenoid protein (OCP) plays a pivotal role in the photoprotection of cyanobacteria and undergoes a structural change after photoactivation. Here, we report a solution structure of the active state differing significantly from that known upon binding to the phycobilisome. In solution, the N-terminal domains are clearly detached and reoriented by about 90° relative to the C- terminal domains. This apparent structural difference implies the need for a previously unknown structural rearrangement. A rarely considered aspect is the internal protein dynamics facilitating this structural transition. Therefore, we directly probe protein dynamics in a wide observation time range in the dark and under illumination. After photoactivation to the active state, the internal dynamics is enhanced, while the global diffusion is slowed down. A residue-resolved molecular dynamics simulation indicates that the interdomain linker becomes more flexible and may mediate the structural adaptation to the phycobilisome binding site. In turn, the β-sheet structures remain the most rigid part of the active state structure, which is essential for protein dimerization.