Structural insights into the oligomerization of FtsH periplasmic domain from Thermotoga maritima

Journal Article · Mon Jan 15 04:00:00 EST 2018 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/J.BBRC.2017.11.158· OSTI ID:23134444

An, Jun Yop; Sharif, Humayun ^[1]; Kang, Gil Bu ^[1]; Park, Kyung Jin; Lee, Jung-Gyu ^[1]; Lee, Sukyeong ^[2]; Jin, Mi Sun ^[1]; Song, Ji-Joon ^[3]; Wang, Jimin ^[4]

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1. School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 61005 (Korea, Republic of)
2. Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030 (United States)
3. Department of Biological Sciences, KI for the BioCentury, Cancer Metastasis Control Center, KAIST, Daejeon 34141 (Korea, Republic of)
4. Steitz Center for Structural Biology, Gwangju Institute of Science and Technology, Gwangju 61005 (Korea, Republic of)

Highlights: • We report the 1.5–1.95A resolution crystal structures of the Thermotoga maritima FtsH periplasmic domain (tmPD). • Acidic residues at the pore region of tmPD are highly conserved among only the thermophilic, FtsH homologs. • The negative charge repulsion of tmPD destabilizes its hexamerization. • Dynamical features of the PD in hexameric full-length FtsH may be relevant for the substrate recognition. 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 Å resolution crystal structures of the Thermotoga maritima FtsH periplasmic domain (tmPD) and describe the dynamic features of tmPD oligomerization.

• OSTI ID: 23134444
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 1 Vol. 495; ISSN BBRCA9; ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
ATP
CRYSTAL STRUCTURE
HOMEOSTASIS
MEMBRANE PROTEINS
QUALITY CONTROL
TOXICITY