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
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出版日期 | 2013 |
卷号 | 69页码:830-837 |
ISSN号 | 2059-7983 |
DOI | 10.1107/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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