Tossavainen Helena, Permi Perttu, Annila Arto, Kilpeläinen Ilkka, Drakenberg Torbjörn
NMR laboratory, Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Finland.
Eur J Biochem. 2003 Jun;270(11):2505-12. doi: 10.1046/j.1432-1033.2003.03623.x.
The structure of calerythrin, a prokaryotic 20 kDa calcium-binding protein has been determined by solution NMR spectroscopy. Distance, dihedral angle, J coupling, secondary chemical shift, residual dipolar coupling and radius of gyration restraints reveal four EF-hand motifs arranged in a compact globular structure. A tight turn in the middle of the amino acid sequence brings the two halves, each comprising a pair of EF-hands, close together. The structural similarity between calerythrin and the eukaryotic sarcoplasmic calcium-binding proteins is notable.
芹菜红素(一种原核生物20 kDa钙结合蛋白)的结构已通过溶液核磁共振光谱法测定。距离、二面角、J耦合、二级化学位移、剩余偶极耦合和回转半径限制揭示了四个EF手基序排列成紧密的球状结构。氨基酸序列中间的一个紧密转角使两半部分(每半部分包含一对EF手)靠近在一起。芹菜红素与真核肌浆钙结合蛋白之间的结构相似性很显著。