Rathner Adriana, Chandra Kousik, Rathner Petr, Horničáková Michaela, Schlagnitweit Judith, Kohoutová Jaroslava, Ettrich Rüdiger, Müller Norbert
Institute of Organic Chemistry, Johannes Kepler University, Altenbergerstraße 69, 4040, Linz, Austria.
Faculty of Science, University of South Bohemia, České Budějovice, Czech Republic.
Biomol NMR Assign. 2015 Oct;9(2):341-6. doi: 10.1007/s12104-015-9606-2. Epub 2015 Apr 23.
PsbP (23 kDa) is an extrinsic eukaryotic protein of photosystem II found in the thylakoid membrane of higher plants and green algae. It has been proven to be indispensable for proper functioning of the oxygen evolving complex. By interaction with other extrinsic proteins (PsbQ, PsbO and PsbR), it modulates the concentration of two cofactors of the water splitting reaction, Ca(2+) and Cl(-). The crystallographic structure of PsbP from Spinacia oleracea lacks the N-terminal part as well as two inner regions which were modelled as loops. Those unresolved parts are believed to be functionally crucial for the binding of PsbP to the thylakoid membrane. In this NMR study we report (1)H, (15)N and (13)C resonance assignments of the backbone and side chain atoms of the PsbP protein. Based on these data, an estimate of the secondary structure has been made. The structural motifs found fit the resolved parts of the crystallographic structure very well. In addition, the complete assignment set provides preliminary insight into the dynamic regions.
PsbP（23千道尔顿）是一种存在于高等植物和绿藻类囊体膜中的光系统II外在真核蛋白。已证明它对于放氧复合体的正常功能不可或缺。通过与其他外在蛋白（PsbQ、PsbO和PsbR）相互作用，它调节水裂解反应的两种辅因子Ca(2+)和Cl(-)的浓度。来自菠菜的PsbP的晶体结构缺少N端部分以及两个被模拟为环的内部区域。据信这些未解析的部分对于PsbP与类囊体膜的结合在功能上至关重要。在这项核磁共振研究中，我们报告了PsbP蛋白主链和侧链原子的(1)H、(15)N和(13)C共振归属。基于这些数据，对二级结构进行了估计。发现的结构基序与晶体结构的解析部分非常吻合。此外，完整的归属集为动态区域提供了初步见解。
