ArticleActa crystallographica. Section D, Biological crystallography2013
The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases.
Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Intricate Structure-Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria.International journal of molecular sciences · 2024Review
- Chloroplasts Protein Quality Control and Turnover: A Multitude of Mechanisms.International journal of molecular sciences · 2022Review
- Differential Roles of the Thylakoid Lumenal Deg Protease Homologs in Chloroplast Proteostasis.Plant physiology · 2018Article
- Insights into the Cyanobacterial Deg/HtrA Proteases.Frontiers in plant science · 2016Article
- D1 fragmentation in photosystem II repair caused by photo-damage of a two-step model.Photosynthesis research · 2015Article
- MET1 is a thylakoid-associated TPR protein involved in photosystem II supercomplex formation and repair in Arabidopsis.The Plant cell · 2015Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 Å 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.
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