8HGQ
The apo-flavodoxin dimer from Synechococcus elongatus PCC 7942
8HGQ の概要
エントリーDOI | 10.2210/pdb8hgq/pdb |
分子名称 | Flavodoxin, PHOSPHATE ION (3 entities in total) |
機能のキーワード | flavodoxin, phosphate binding, redox potential, electron transport, fmn binding |
由来する生物種 | Synechococcus elongatus PCC 7942 = FACHB-805 (Anacystis nidulans R2) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 20876.59 |
構造登録者 | |
主引用文献 | Liu, S.,Chen, Y.,Du, T.,Zhao, W.,Liu, X.,Zhang, H.,Yuan, Q.,Gao, L.,Dong, Y.,Gao, X.,Gong, Y.,Cao, P. A dimer-monomer transition captured by the crystal structures of cyanobacterial apo flavodoxin. Biochem.Biophys.Res.Commun., 639:134-141, 2022 Cited by PubMed Abstract: In cyanobacteria and algae (but not plants), flavodoxin (Fld) replaces ferredoxin (Fd) under stress conditions to transfer electrons from photosystem I (PSI) to ferredoxin-NADP reductase (FNR) during photosynthesis. Fld constitutes a small electron carrier noncovalently bound to flavin mononucleotide (FMN), and also an ideal model for revealing the protein/flavin-binding mechanism because of its relative simplicity compared to other flavoproteins. Here, we report two crystal structures of apo-Fld from Synechococcus sp. PCC 7942, one dimeric structure of 2.09 Å and one monomeric structure of 1.84 Å resolution. Analytical ultracentrifugation showed that in solution, apo-Fld exists both as monomers and dimers. Our dimer structure contains two ligand-binding pockets separated by a distance of 45 Å, much longer than the previous structures of FMN-bound dimers. These results suggested a potential dimer-monomer transition mechanism of cyanobacterial apo-Fld. We further propose that the dimer represents the "standby" state to stabilize itself, while the monomer constitutes the "ready" state to bind FMN. Furthermore, we generated a new docking model of cyanobacterial Fld-FNR complex based on the recently reported cryo-EM structures, and mapped the special interactions between Fld and FNR in detail. PubMed: 36493556DOI: 10.1016/j.bbrc.2022.11.089 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.09 Å) |
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