7djl | pdb_00007djl
Structure of four truncated and mutated forms of quenching protein
Structural highlights
FunctionSOQ1_ARATH Required to maintain light harvesting efficiency, especially during nonphotochemical quenching (NPQ) recovery, via the regulation of chlorophyll excited-state lifetime probably by preventing the formation of a slowly reversible form of antenna quenching.[1] Publication Abstract from PubMedNon-photochemical quenching (NPQ) plays an important role for phototrophs in decreasing photo-oxidative damage. qH is a sustained form of NPQ and depends on the plastid lipocalin (LCNP). A thylakoid membrane-anchored protein SUPPRESSOR OF QUENCHING1 (SOQ1) prevents qH formation by inhibiting LCNP. SOQ1 suppresses qH with its lumen-located thioredoxin (Trx)-like and NHL domains. Here we report structural data, genetic modification and biochemical characterization of Arabidopsis SOQ1 lumenal domains. Our results show that the Trx-like and NHL domains are associated together, with the cysteine motif located at their interface. Residue E859, required for SOQ1 function, is pivotal for maintaining the Trx-NHL association. Importantly, the C-terminal region of SOQ1 forms an independent beta-stranded domain that has structural homology to the N-terminal domain of bacterial disulfide bond protein D and is essential for negative regulation of qH. Furthermore, SOQ1 is susceptible to cleavage at the loops connecting the neighbouring lumenal domains both in vitro and in vivo, which could be a regulatory process for its suppression function of qH. Structure of Arabidopsis SOQ1 lumenal region unveils C-terminal domain essential for negative regulation of photoprotective qH.,Yu G, Hao J, Pan X, Shi L, Zhang Y, Wang J, Fan H, Xiao Y, Yang F, Lou J, Chang W, Malnoe A, Li M Nat Plants. 2022 Jul;8(7):840-855. doi: 10.1038/s41477-022-01177-z. Epub 2022 Jul , 7. PMID:35798975[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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