1H and 15N NMR assignments of PsaE, a photosystem I subunit from the cyanobacterium Synechococcus sp. strain PCC 7002.
1H and 15N NMR assignments of PsaE, a photosystem I subunit from the cyanobacterium Synechococcus sp. strain PCC 7002.
复制标题
PsaE 的 1H 和 15N NMR 归属，PsaE 是蓝藻聚球藻属的光系统 I 亚基。
DOI：
10.1021/bi00186a003
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发表时间：
1994
期刊：
影响因子：
2.9
通讯作者：
Lecomte,JT
中科院分区：
文献类型：
--
作者：
Falzone,CJ;Kao,YH;Zhao,J;MacLaughlin,KL;Bryant,DA;Lecomte,JT
修订稿于 1994 年 3 月 9 日收到® 摘要：PsaE 是蓝藻、藻类和绿色植物的光系统 I 反应中心复合物的高度保守的水溶性蛋白质。 PsaE 蛋白与 PsaC 和 PsaD 蛋白一起结合到光系统 I 的基质表面，并且是聚球藻中循环电子传输所必需的。菌株 PCC 7002 [Yu, L.、Zhao, J.、Mühlenhoff, U.、Bryant, D. A. 和 Golbeck, J. H.(1993) 植物生理学。 103、171-180]。来自这种蓝藻的 psaE 基因编码 69 个氨基酸残基的成熟蛋白，最近在大肠杆菌中过表达 [Zhao, J., Snyder, W. B., Mühlenhoff, U., Rhiel, E., Warren, P. V., Golbeck, J. H., & Bryant, D. A.(1993) Mol.微生物。 9、183-194]。通过在一系列二维和三维 NMR 实验中使用未标记和统一 15N 标记的蛋白质，完成了完整的 15N 酰胺共振分配。 PsaE 的主要二级结构元件是五链反平行/3 片。 5条链延伸如下：/3A，残基7-10；/3B，残基21-26；/3C，残基36-39；/3D，残基57-60；/3D，残基57-60。和/3E，残基65-68。拓扑结构用(+1,+1,+1,-4x)表示；它将第一条链和最后一条链，以及 N 端和 C 端连接在一起。该蛋白质具有围绕保守的苯丙氨酸残基 (Phe-40) 组织的广泛疏水核心；其另一个显着特征是从残基42延伸到残基56的区段，没有与/3-片的偶极接触。唯一组氨酸残基 (His-63) 的 pÁj/2 确定为 5.4。PsaE1 蛋白是光系统 I (PS I) 反应中心复合体的亚基，存在于所有释氧光合生物中，包括蓝细菌、真核藻类和高等植物。 PS I 充当膜结合的光氧化还原酶，并催化光驱动的电子从还原质体蓝蛋白（或细胞色素，例如）转移到氧化铁氧还蛋白[或黄素氧还蛋白；有关评论，请参阅 Bryant (1992)、Chitnis 和 Nelson (1991)、Golbeck (1992、1994) 以及 Golbeck 和 Bryant (1991)]。蓝藻PS I复合物由11个多肽亚基、约100个叶绿素a分子、10-15个d-胡萝卜素、2个维生素Ki分子和3个[4Fe-4S]中心（表示为Fx、Fa和Fb）组成。 PsaE 亚基与 PS I 复合物 (P700-Fx) 核心蛋白的基质侧相关（Li 等人，1991a；Parrett 等人，1990）。来自蓝藻聚球藻属的 PsaC、PsaD 和 PsaE。 PCC 7002 在大肠杆菌中过量生产并用于体外重构研究
Revised Manuscript Received March 9, 1994® abstract: PsaE is a highly conserved, water-solubleprotein of the photosystem I reaction center complexes of cyanobacteria, algae, and green plants. Along with the PsaC and PsaD proteins, the PsaE protein binds to the stromal surface of photosystem I and is requiredfor cyclic electron transport in Synechococcus sp. strain PCC 7002 [Yu, L., Zhao, J., Mühlenhoff, U., Bryant, D. A., & Golbeck, J. H.(1993) Plant Physiol. 103, 171-180]. The psaE gene from this cyanobacterium encodes a mature protein of 69 amino acid residues and has recently been overexpressed in Escherichia coli [Zhao, J., Snyder, W. B., Mühlenhoff, U., Rhiel, E., Warren, P. V., Golbeck, J. H., & Bryant, D. A.(1993) Mol. Microbiol. 9, 183-194]. By using both unlabeled and uniformly 15N-labeled protein in a series of two-and three-dimensional NMR experiments, complete and 15N amide resonance assignments were made. The major secondary structural element of PsaE is a five-stranded antiparallel/3-sheet. The five strands extend as follows:/3A, residues 7-10;/3B, residues 21-26;/3C, residues 36-39;/3D, residues 57-60; and/3E, residues 65-68. The topology is represented by (+ 1,+ 1,+ 1,-4x); it brings the first and last strands, and consequently the N-and C-termini, together. The protein has an extensive hydrophobic core organized around a conserved phenylalanine residue (Phe-40); another of its distinctive features is a segment extending from residue 42 to residue 56 devoid of dipolar contacts with the/3-sheet. The pÁj/2 of the sole histidine residue (His-63) was determined to be 5.4.The PsaE1 protein is a subunit of the photosystem I (PS I) reaction center complex that is found in all oxygen-evolving photosynthetic organisms, including cyanobacteria, eukaryotic algae, and higher plants. PS I functions as a membrane-bound, photooxidoreductase and catalyzes the light-driven transfer of an electron from reduced plastocyanin (or cytochrome eg) to oxidized ferredoxin [or flavodoxin; for reviews, see Bryant (1992), Chitnis and Nelson (1991), Golbeck (1992, 1994), and Golbeck and Bryant (1991)]. The cyanobacterial PS I complex is made up of 11 polypeptide subunits, about 100 chlorophyll a molecules, 10-15 d-carotenes, 2 vitamin Ki molecules, and 3 [4Fe-4S] centers denoted Fx, Fa, and Fb. The PsaE subunit is associated with the stromal side of the PS I complex (P700-Fx) core protein (Li etal., 1991a; Parrett etal., 1990). PsaC, PsaD, and PsaE from the cyanobacterium Synechococcus sp. PCC 7002have been overproduced in Escherichia coli andused in reconstitution studies in vitro