Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum
Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum
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DOI：
10.1038/sj.embor.7400113
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发表时间：
2004-04-01
期刊：
影响因子：
7.7
通讯作者：
Sato, F
中科院分区：
文献类型：
--
作者：
Ifuku, K;Nakatsu, T;Sato, F
PsbP是水氧化复合光系统II （PS II）的膜外亚基。PsbP的进化起源长期以来一直是个谜，因为它只存在于高等植物和绿藻中，而不存在于蓝藻中。本文报道了烟草中PsbP的晶体结构，分辨率为1.6埃。其结构主要由β -sheet组成，与蓝藻PS II中的任何结构都不相似。但PsbP的静电表面电位与蓝藻细菌PsbV （cyt c(550)）相似，具有与PsbP相似的功能。利用DALI算法进行结构同源性搜索，发现PsbP的折叠与Ran GTPase核转运调节蛋白Mog1p的折叠非常相似。PsbP的结构揭示了其在PS II中gtp调控代谢中的新功能。
PsbP is a membrane-extrinsic subunit of the water-oxidizing complex photosystem II (PS II). The evolutionary origin of PsbP has long been a mystery because it specifically exists in higher plants and green algae but not in cyanobacteria. We report here the crystal structure of PsbP from Nicotiana tabacum at a resolution of 1.6 Angstrom. Its structure is mainly composed of beta-sheet, and is not similar to any structures in cyanobacterial PS II. However, the electrostatic surface potential of PsbP is similar to that of cyanobacterial PsbV (cyt c(550)), which has a function similar to PsbP. A structural homology search with the DALI algorithm indicated that the folding of PsbP is very similar to that of Mog1p, a regulatory protein for the nuclear transport of Ran GTPase. The structure of PsbP provides insight into its novel function in GTP-regulated metabolism in PS II.