中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases

文献类型:期刊论文

作者Sun, Wei1; Gao, Feng; Fan, Haitian1; Shan, Xiaoyue1; Sun, Renhua1,3; Liu, Lin3; Gong, Weimin
刊名ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
出版日期2013
卷号69页码:830-837
ISSN号2059-7983
DOI10.1107/S0907444913002023
文献子类Article
英文摘要Plant Deg5 and Deg8 are two members of the HtrA proteases, a family of oligomeric serine endopeptidases that are involved in a variety of protein quality-control processes. These two HtrA proteases are located in the thylakoid lumen and participate in high-light stress responses by collaborating with other chloroplast proteins. Deg5 and Deg8 degrade photodamaged D1 protein of the photosystem II reaction centre, allowing its in situ replacement. Here, the crystal structures of Arabidopsis thaliana Deg5 (S266A) and Deg8 (S292A) are reported at 2.6 and 2.0 angstrom resolution, respectively. The Deg5 trimer contains two calcium ions in a central channel, suggesting a link between photodamage control and calcium ions in chloroplasts. Previous structures of HtrA proteases have indicated that their regulation usually requires C-terminal PDZ domain(s). Deg5 is unique in that it contains no PDZ domain and the trimeric structure of Deg5 (S266A) reveals a novel catalytic triad conformation. A similar triad conformation is observed in the hexameric structure of the single PDZ-domain-containing Deg8 (S292A). These findings suggest a novel activation mechanism for plant HtrA proteases and provide structural clues to their function in light-stress response.
学科主题Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biophysics ; Crystallography
出版地CHESTER
WOS关键词PHOTOSYSTEM-II ; CRYSTAL-STRUCTURE ; MOLECULAR REPLACEMENT ; STRESS SENSOR ; D1 PROTEIN ; REPAIR ; DEGRADATION ; ACTIVATION ; FAMILY ; PHOTOINHIBITION
WOS研究方向Science Citation Index Expanded (SCI-EXPANDED)
语种英语
WOS记录号WOS:000318240200017
出版者INT UNION CRYSTALLOGRAPHY
资助机构Ministry of Science and Technology of China(Ministry of Science and Technology, China) ; National Natural Science Foundation of China(National Natural Science Foundation of China (NSFC))
源URL[http://ir.ibcas.ac.cn/handle/2S10CLM1/27903]  
专题中科院光生物学重点实验室
作者单位1.Chinese Acad Sci, Inst Bot, Photosynth Res Ctr, Key Lab Photobiol, Beijing 100093, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Chinese Acad Sci, Inst Biophys, Lab Noncoding RNA, Beijing 100101, Peoples R China
推荐引用方式
GB/T 7714
Sun, Wei,Gao, Feng,Fan, Haitian,et al. The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases[J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY,2013,69:830-837.
APA Sun, Wei.,Gao, Feng.,Fan, Haitian.,Shan, Xiaoyue.,Sun, Renhua.,...&Gong, Weimin.(2013).The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases.ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY,69,830-837.
MLA Sun, Wei,et al."The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases".ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 69(2013):830-837.

入库方式: OAI收割

来源:植物研究所

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