Structural insights into the oligomerization of FtsH periplasmic domain from Thermotoga maritima
| Autor: | Jun Yop An, Ji-Joon Song, Jimin Wang, Soo Hyun Eom, Kyung Jin Park, Sukyeong Lee, Gil Bu Kang, Jung-Gyu Lee, Humayun Sharif, Mi Sun Jin |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Models Molecular Protein Conformation medicine.medical_treatment Protein domain Biophysics Plasma protein binding Biochemistry 03 medical and health sciences Structure-Activity Relationship Protein structure ATP-Dependent Proteases Protein Domains medicine Computer Simulation Thermotoga maritima Molecular Biology Protease Binding Sites biology Chemistry Cell Biology Periplasmic space biology.organism_classification Transmembrane protein Enzyme Activation 030104 developmental biology Membrane protein Models Chemical bacteria Protein Multimerization Peptide Hydrolases Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 495(1) |
| ISSN: | 1090-2104 |
| Popis: | Prompt removal of misfolded membrane proteins and misassembled membrane protein complexes is essential for membrane homeostasis. However, the elimination of these toxic proteins from the hydrophobic membrane environment has high energetic barriers. The transmembrane protein, FtsH, is the only known ATP-dependent protease responsible for this task. The mechanisms by which FtsH recognizes, unfolds, translocates, and proteolyzes its substrates remain unclear. The structure and function of the ATPase and protease domains of FtsH have been previously characterized while the role of the FtsH periplasmic domain has not clearly identified. Here, we report the 1.5-1.95 A resolution crystal structures of the Thermotoga maritima FtsH periplasmic domain (tmPD) and describe the dynamic features of tmPD oligomerization. |
| Databáze: | OpenAIRE |
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