• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

结构异质性导致海洋鱼腥藻藻蓝蛋白功能的均一性。

Structural heterogeneity leads to functional homogeneity in A. marina phycocyanin.

机构信息

Schulich Faculty of Chemistry, Technion-Israel Institute of Technology, Haifa 32000, Israel.

Photosythetic Antenna Research Center, Washington University in St. Louis, St. Louis, MO 63130, USA.

出版信息

Biochim Biophys Acta Bioenerg. 2018 Jul;1859(7):544-553. doi: 10.1016/j.bbabio.2018.04.007. Epub 2018 Apr 25.

DOI:10.1016/j.bbabio.2018.04.007
PMID:29704497
Abstract

The major light harvesting antenna in all cyanobacterial species is the phycobilisome (PBS). The smallest PBS identified to date is that of Acaryochloris marina (A. marina), composed of a single four-hexamer rod. We have determined the crystal structure of phycocyanin (AmPC), the major component of the A. marina PBS (AmPBS) to 2.1 Å. The basic unit of the AmPC is a heterodimer of two related subunits (α and β), and we show that the asymmetric unit contains a superposition of two α and two β isoforms, the products of the simultaneous expression of different genes. This is the first time to our knowledge that isolated proteins crystallized with such identifiable heterogeneity. We believe that the presence of the different isoforms allows the AmPBS to have a significant bathochromic shift in its fluorescence emission spectrum, allowing, in the total absence of allophycocyanin, a better overlap with absorption of the chlorophyll d-containing reaction centers. We show that this bathochromic shift exists in intact AmPBS as well as in its disassembled components, thus suggesting that AmPC can efficiently serve as the AmPBS terminal emitter.

摘要

所有蓝细菌物种的主要光收集天线是藻胆体(PBS)。迄今为止鉴定出的最小 PBS 是海洋鱼腥藻(A. marina)的 PBS,由单个四聚体棒组成。我们已经确定了藻蓝蛋白(AmPC)的晶体结构,藻蓝蛋白是 A. marina PBS(AmPBS)的主要成分,分辨率为 2.1Å。AmPC 的基本单元是两个相关亚基(α和β)的异源二聚体,我们表明,不对称单元包含两个α和两个β同种型的叠加,这是同时表达不同基因的产物。据我们所知,这是首次在分离的蛋白质结晶中出现这种可识别的异质性。我们认为不同同种型的存在使得 AmPBS 在其荧光发射光谱中具有显著的红移,从而在完全没有别藻蓝蛋白的情况下,与含有叶绿素 d 的反应中心的吸收更好地重叠。我们表明,这种红移不仅存在于完整的 AmPBS 中,也存在于其拆开的组件中,因此表明 AmPC 可以有效地作为 AmPBS 的末端发射器。

相似文献

1
Structural heterogeneity leads to functional homogeneity in A. marina phycocyanin.结构异质性导致海洋鱼腥藻藻蓝蛋白功能的均一性。
Biochim Biophys Acta Bioenerg. 2018 Jul;1859(7):544-553. doi: 10.1016/j.bbabio.2018.04.007. Epub 2018 Apr 25.
2
Isolation and characterization of biliprotein aggregates from Acaryochloris marina, a Prochloron-like prokaryote containing mainly chlorophyll d.从主要含有叶绿素d的类原绿球藻的原绿球藻样原核生物——滨海蓝藻中分离和鉴定藻胆蛋白聚集体。
FEBS Lett. 1997 Jun 30;410(2-3):428-32. doi: 10.1016/s0014-5793(97)00631-5.
3
Molecular structure, localization and function of biliproteins in the chlorophyll a/d containing oxygenic photosynthetic prokaryote Acaryochloris marina.含叶绿素a/d的产氧光合原核生物滨海栖热放线菌中藻胆蛋白的分子结构、定位及功能
Biochim Biophys Acta. 1999 Aug 4;1412(3):250-61. doi: 10.1016/s0005-2728(99)00067-5.
4
High-resolution crystal structures of trimeric and rod phycocyanin.三聚体和棒状藻蓝蛋白的高分辨率晶体结构。
J Mol Biol. 2011 Jan 7;405(1):201-13. doi: 10.1016/j.jmb.2010.10.036. Epub 2010 Oct 28.
5
Low absorption state of phycocyanin from Acaryochloris marina antenna system: on the interplay between ionic strength and excitonic coupling.海洋聚球藻天线系统藻蓝蛋白低吸收态:离子强度与激子耦合的相互作用。
J Chem Phys. 2013 Jul 28;139(4):045101. doi: 10.1063/1.4813803.
6
Crystal structure of a light-harvesting protein C-phycocyanin from Spirulina platensis.钝顶螺旋藻捕光蛋白C-藻蓝蛋白的晶体结构。
Biochem Biophys Res Commun. 2001 Apr 13;282(4):893-8. doi: 10.1006/bbrc.2001.4663.
7
Structural studies show energy transfer within stabilized phycobilisomes independent of the mode of rod-core assembly.结构研究表明,在稳定的藻胆体中存在能量转移,且与棒状核心组装模式无关。
Biochim Biophys Acta. 2014 Mar;1837(3):385-95. doi: 10.1016/j.bbabio.2013.12.014. Epub 2014 Jan 6.
8
Crystallization and preliminary X-ray diffraction analysis of the light-harvesting protein phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus.嗜热蓝藻聚球藻中光捕获蛋白藻蓝蛋白的结晶及初步X射线衍射分析
Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1326-8. doi: 10.1107/s0907444901011969. Epub 2001 Aug 23.
9
Excitation energy transfer and electron-vibrational coupling in phycobiliproteins of the cyanobacterium Acaryochloris marina investigated by site-selective spectroscopy.通过位点选择性光谱研究蓝藻菌滨海栖热袍菌藻胆蛋白中的激发能量转移和电子 - 振动耦合。
Biochim Biophys Acta. 2014 Sep;1837(9):1490-9. doi: 10.1016/j.bbabio.2014.02.010. Epub 2014 Feb 21.
10
Crystal structure of phycocyanin from heterocyst-forming filamentous cyanobacterium Nostoc sp. WR13.异形胞形成丝状蓝藻 Nostoc sp. WR13 藻蓝蛋白的晶体结构。
Int J Biol Macromol. 2019 Aug 15;135:62-68. doi: 10.1016/j.ijbiomac.2019.05.099. Epub 2019 May 20.

引用本文的文献

1
Acclimation to white light in a far-red light specialist: insights from Acaryochloris marina MBIC11017.远红光专家对白光的适应性:来自滨海蓝藻菌MBIC11017的见解
New Phytol. 2025 Jul;247(1):128-143. doi: 10.1111/nph.70188. Epub 2025 May 5.
2
Integration of horizontally acquired light-harvesting genes into an ancestral regulatory network in the cyanobacterium MBIC11017.水平获得的光捕获基因整合到蓝细菌MBIC11017的祖先调控网络中。
mBio. 2024 Dec 11;15(12):e0242324. doi: 10.1128/mbio.02423-24. Epub 2024 Nov 18.
3
Duplicate Gene Expression and Possible Mechanisms of Paralog Retention During Bacterial Genome Expansion.
细菌基因组扩张过程中重复基因表达及其可能的旁系同源物保留机制。
Genome Biol Evol. 2024 May 2;16(5). doi: 10.1093/gbe/evae089.
4
Exploring the structural aspects and therapeutic perspectives of cyanobacterial phycobiliproteins.探索蓝藻藻胆蛋白的结构方面和治疗前景。
3 Biotech. 2022 Sep;12(9):224. doi: 10.1007/s13205-022-03284-2. Epub 2022 Aug 13.
5
Non-conventional octameric structure of C-phycocyanin.C 藻蓝蛋白的非常规八聚体结构。
Commun Biol. 2021 Oct 29;4(1):1238. doi: 10.1038/s42003-021-02767-x.
6
Revisiting high-resolution crystal structure of Phormidium rubidum phycocyanin.重访鱼腥藻藻蓝蛋白的高分辨率晶体结构。
Photosynth Res. 2020 Jun;144(3):349-360. doi: 10.1007/s11120-020-00746-7. Epub 2020 Apr 17.