8XF1
Crystal structure of the dissociated C-phycocyanin beta-chain from Thermoleptolyngbya sp. O-77
8XF1 の概要
エントリーDOI | 10.2210/pdb8xf1/pdb |
分子名称 | C-phycocyanin beta chain, PHYCOCYANOBILIN (3 entities in total) |
機能のキーワード | dissociated subunit, c-phycocyanin, photosynthesis |
由来する生物種 | Leptolyngbya sp. O-77 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 19274.85 |
構造登録者 | |
主引用文献 | Nguyen, H.K.,Minato, T.,Teramoto, T.,Ogo, S.,Kakuta, Y.,Yoon, K.S. Disassembly and reassembly of the non-conventional thermophilic C-phycocyanin. J.Biosci.Bioeng., 137:179-186, 2024 Cited by PubMed Abstract: C-phycocyanin (CPC), which contains open-chain tetrapyrroles, is a major light-harvesting red-fluorescent protein with an important role in aquatic photosynthesis. Recently, we reported a non-conventional CPC from Thermoleptolyngbya sp. O-77 (CPC) that contains two different structures, i.e., a hexameric structure and a non-conventional octameric structure. However, the assembly and disassembly mechanisms of the non-conventional octameric form of CPC remain unclear. To understand this assembly mechanism, we performed an in vitro experiment to study the disassembly and reassembly behaviors of CPC using isolated CPC subunits. The dissociation of the CPC subunit was performed using a Phenyl-Sepharose column in 20 mM potassium phosphate buffer (pH 6.0) containing 7.0 M urea. For the first time, crystals of isolated CPC subunits were obtained and analyzed after separation. After the removal of urea from the purified α and β subunits, we performed an in vitro reassembly experiment for CPC and analyzed the reconstructed CPC using spectrophotometric and X-ray crystal structure analyses. The crystal structure of the reassembled CPC was nearly identical to that of the original CPC. The findings of this study indicate that the octameric CPC is a naturally occurring form in the thermophilic cyanobacterium Thermoleptolyngbya sp. O-77. PubMed: 38238241DOI: 10.1016/j.jbiosc.2023.12.015 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.94 Å) |
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