1KTP

Crystal structure of c-phycocyanin of synechococcus vulcanus at 1.6 angstroms

1KTP の概要

• エントリーDOI: 10.2210/pdb1ktp/pdb
• 関連するPDBエントリー: 1I7Y
• 分子名称: C-PHYCOCYANIN ALPHA SUBUNIT, C-PHYCOCYANIN BETA SUBUNIT, BILIVERDINE IX ALPHA, ... (5 entities in total)
• 機能のキーワード: cyanobacteria, photosynthesis, photosystem ii, light harvesting proteins, thermostability
• 由来する生物種: Thermosynechococcus vulcanus; 詳細
• 細胞内の位置: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P50032 P50033
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37447.34

構造登録者

Adir, N.,Dobrovetsky, E.,Lerner, N. (登録日: 2002-01-17, 公開日: 2002-03-06, 最終更新日: 2023-08-16)

主引用文献

Adir, N.,Vainer, R.,Lerner, N.
Refined structure of c-phycocyanin from the cyanobacterium Synechococcus vulcanus at 1.6 A: insights into the role of solvent molecules in thermal stability and co-factor structure
Biochim.Biophys.Acta, 1556:168-174, 2002

PubMed Abstract: The crystal structure of the light-harvesting phycobiliprotein, c-phycocyanin from the thermophilic cyanobacterium Synechococcus vulcanus has been refined to 1.6 A resolution based on the previously determined lower resolution structure (PDB entry 1I7Y). The improved data was collected using synchrotron radiation at 100 K. The significantly improved crystallographic data has lead to improved calculated electron density maps, allowing the unambiguous positioning of all protein and co-factor atoms and the positioning of 377 solvent molecules. The positions of solvent molecules at specific sites important for stabilization of different levels of self-assembly of the phycobilisome structure were identified and the bonding network is described. The presence of solvent molecules in the vicinity of the co-factors and in intermolecular spaces is identified and their possible roles are suggested. All three of the phycocyanobilin co-factors bind water molecules at specific sites between the propionic acid side chains. Molecular dynamic (MD) simulations support that these special waters have a role in stabilization of this conformation. On the basis of the crystal packing reported here and in comparison to other phycobiliprotein crystal forms, we have analyzed the roles of specific sites on the formation of the phycobilisome complex.

PubMed: 12460674
DOI: 10.1016/S0005-2728(02)00359-6

実験手法

X-RAY DIFFRACTION (1.6 Å)