High-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium, Synechocystis sp. PCC 6803.
High-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium, Synechocystis sp. PCC 6803.
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DOI：
10.1073/pnas.2116765118
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发表时间：
2022-01-04
影响因子：
11.1
通讯作者：
Brudvig GW
中科院分区：
文献类型：
--
作者：
Gisriel CJ;Wang J;Liu J;Flesher DA;Reiss KM;Huang HL;Yang KR;Armstrong WH;Gunner MR;Batista VS;Debus RJ;Brudvig GW
光系统II （PSII）是一种利用光能利用水制造燃料的光氧化还原酶。水氧化发生在活性部位的金属簇上，称为出氧络合物（OEC）。了解PSII功能为合成太阳能燃料催化剂提供了设计原则；然而，水氧化的细节被机制进行的多种状态、物种之间的差异和OEC的稳定性所掩盖。为了更好地理解PSII的功能，我们从Synechocystis sp. PCC 6803中求解了PSII的结构。我们观察到与来自嗜热蓝藻的PSII相比存在显著差异，这突出了使用该结构重新检查先前数据的必要性。该结构也为PSII位点定向突变的研究提供了一个平台。光系统II （PSII）可以实现全球范围的光驱动水氧化。对中温蓝藻胞藻PSII的基因操作为水氧化机制的研究提供了新的思路；然而，由于缺乏该生物进化氧PSII的高分辨率结构，限制了对生物物理数据的解释，使其仅限于基于嗜热蓝藻PSII结构的模型。在这里，我们报道了Synechocystis sp. PCC 6803 PSII的低温电镜结构，分辨率为1.93-Å。与热性PSII结构相比，观察到许多差异，包括以下方面：外部亚基PsbQ被维持，D1亚基的C端是柔性的，活性位点附近的一些水被部分占据，PsbV亚基的差异阻断了大（O1）水通道。这些特征强烈地影响了PSII的结构图，特别是它与水氧化机制有关。
Photosystem II (PSII) is a photo-oxidoreductase that harnesses light energy to use water to make fuel. Water oxidation occurs at a metal cluster in the active site called the oxygen-evolving complex (OEC). Understanding PSII function has provided design principles for synthetic solar fuel catalysts; however, the details of water oxidation are obscured by the multiple states through which the mechanism proceeds, differences between species, and lability of the OEC. To better understand PSII function, we solved its structure from Synechocystis sp. PCC 6803. We observe significant differences compared with PSII from thermophilic cyanobacteria that highlight the need for reexamination of previous data using this structure for interpretation. The structure also provides a platform for studies of site-directed mutations of PSII. Photosystem II (PSII) enables global-scale, light-driven water oxidation. Genetic manipulation of PSII from the mesophilic cyanobacterium Synechocystis sp. PCC 6803 has provided insights into the mechanism of water oxidation; however, the lack of a high-resolution structure of oxygen-evolving PSII from this organism has limited the interpretation of biophysical data to models based on structures of thermophilic cyanobacterial PSII. Here, we report the cryo-electron microscopy structure of PSII from Synechocystis sp. PCC 6803 at 1.93-Å resolution. A number of differences are observed relative to thermophilic PSII structures, including the following: the extrinsic subunit PsbQ is maintained, the C terminus of the D1 subunit is flexible, some waters near the active site are partially occupied, and differences in the PsbV subunit block the Large (O1) water channel. These features strongly influence the structural picture of PSII, especially as it pertains to the mechanism of water oxidation.
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影响因子：
16.8
作者：
Guskov, Albert;Kern, Jan;Saenger, Wolfram
通讯作者：
Saenger, Wolfram
影响因子：
4.4
作者：
BECKE, AD
通讯作者：
BECKE, AD
DOI：
10.1107/s2059798318006551
发表时间：
2018-06-01
期刊：
Acta crystallographica. Section D, Structural biology
影响因子：
--
作者：
Afonine PV;Poon BK;Read RJ;Sobolev OV;Terwilliger TC;Urzhumtsev A;Adams PD
通讯作者：
Adams PD
影响因子：
2.9
作者：
Debus, Richard J.
通讯作者：
Debus, Richard J.
S1至S2转变引起的光系统II的氧气发展复合物的结构变化：XRD和QM/MM研究的组合。
影响因子：
2.9
作者：
Askerka, Mikhail;Wang, Jimin;Brudvig, Gary W.;Batista, Victor S.
通讯作者：
Batista, Victor S.