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The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases
Sun, Wei2; Gao, Feng; Fan, Haitian2; Shan, Xiaoyue2; Sun, Renhua1,2; Liu, Lin1; Gong, Weimin
2013
发表期刊ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
ISSN2059-7983
卷号69页码:830-837
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.
学科领域Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biophysics ; Crystallography
DOI10.1107/S0907444913002023
收录类别SCI
语种英语
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)
WOS记录号WOS:000318240200017
出版者INT UNION CRYSTALLOGRAPHY
Special IssueSI
文献子类Article
出版地CHESTER
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))
作品OA属性hybrid, Green Published, Green Accepted
引用统计
被引频次:13[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符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 Biophys, Lab Noncoding RNA, Beijing 100101, Peoples R China
2.Chinese Acad Sci, Inst Bot, Photosynth Res Ctr, Key Lab Photobiol, Beijing 100093, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
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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.
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