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

被引:2
作者
An, Jun Yop [1 ,2 ]
Sharif, Humayun [1 ,2 ,6 ,7 ]
Kang, Gil Bu [1 ,8 ]
Park, Kyung Jin [1 ,2 ]
Lee, Jung-Gyu [1 ,2 ]
Lee, Sukyeong [3 ]
Jin, Mi Sun [1 ]
Song, Ji-Joon [4 ]
Wang, Jimin [2 ,5 ]
Eom, Soo Hyun [1 ,2 ]
机构
[1] Gwangju Inst Sci & Technol, Sch Life Sci, Gwangju 61005, South Korea
[2] Gwangju Inst Sci & Technol, Steitz Ctr Struct Biol, Gwangju 61005, South Korea
[3] Baylor Coll Med, Verna & Marrs McLean Dept Biochem & Mol Biol, Houston, TX 77030 USA
[4] Korea Adv Inst Sci & Technol, Canc Metastasis Control Ctr, KI BioCentury, Dept Biol Sci, Daejeon 34141, South Korea
[5] Yale Univ, Dept Mol Biophys & Biochem, POB 6666, New Haven, CT 06520 USA
[6] Dana Farber Canc Inst, Dept Canc Biol, 450 Brookline Ave, Boston, MA 02215 USA
[7] Harvard Med Sch, Dept Biol Chem & Mol Pharmacol, Boston, MA 02215 USA
[8] GreenCross Inc, Res & Dev Ctr, Ihyeon Ro 30 Beon Gil, Yonginsi Si 16924, Gyeonggi Do, South Korea
基金
新加坡国家研究基金会;
关键词
ATP-Dependent protease; Membrane protein quality control; Crystal structure; FtsH; Periplasmic domain; ATP-DEPENDENT PROTEASE; QUALITY-CONTROL; PHOTOSYSTEM-II; MEMBRANE; LOCALIZATION; SUBSTRATE; COMPLEX;
D O I
10.1016/j.bbrc.2017.11.158
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 angstrom resolution crystal structures of the Thermotoga maritima FtsH periplasmic domain (tmPD) and describe the dynamic features of tmPD oligomerization. (C) 2017 Elsevier Inc. All rights reserved.
引用
收藏
页码:1201 / 1207
页数:7
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