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

Biochem Biophys Res Commun. 2018 Jan 1;495(1):1201-1207. doi: 10.1016/j.bbrc.2017.11.158. Epub 2017 Nov 24.

Abstract

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.

Keywords: ATP-Dependent protease; Crystal structure; FtsH; Membrane protein quality control; Periplasmic domain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Dependent Proteases / chemistry*
  • ATP-Dependent Proteases / ultrastructure*
  • Binding Sites
  • Computer Simulation
  • Enzyme Activation
  • Models, Chemical
  • Models, Molecular
  • Peptide Hydrolases / chemistry*
  • Peptide Hydrolases / ultrastructure*
  • Protein Binding
  • Protein Conformation
  • Protein Domains
  • Protein Multimerization*
  • Structure-Activity Relationship
  • Thermotoga maritima / enzymology*

Substances

  • Peptide Hydrolases
  • ATP-Dependent Proteases