Preprint Article Version 1 This version is not peer-reviewed

Structural Insights into Thermotoga maritima FtsH Periplasmic Domain on Substrate Recognition

Version 1 : Received: 29 December 2016 / Approved: 29 December 2016 / Online: 29 December 2016 (17:16:52 CET)

How to cite: An, J.Y.; Sharif, H.; Kang, G.B.; Park, K.J.; Lee, J.; Lee, S.; Jin, M.S.; Song, J.; Wang, J.; Eom, S.H. Structural Insights into Thermotoga maritima FtsH Periplasmic Domain on Substrate Recognition. Preprints 2016, 2016120145 (doi: 10.20944/preprints201612.0145.v1). An, J.Y.; Sharif, H.; Kang, G.B.; Park, K.J.; Lee, J.; Lee, S.; Jin, M.S.; Song, J.; Wang, J.; Eom, S.H. Structural Insights into Thermotoga maritima FtsH Periplasmic Domain on Substrate Recognition. Preprints 2016, 2016120145 (doi: 10.20944/preprints201612.0145.v1).

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. Transmembrane FtsH is the only known ATP-dependent protease responsible for this task, unlike other well-studied soluble ATP-dependent proteases. The mechanisms by which FtsH recognizes, unfolds, translocates, and proteolyzes its substrates remain unclear. Here, we report the crystal structures of the Thermotoga maritima FtsH periplasmic domain (PD) in an associative trimeric state at a 1.5-1.95 Å resolution. We also describe the pH-dependent oligomerization states of the isolated PD using dynamic light scattering. These observations help us understand how FtsH recognizes membrane-anchored misfolded proteins.

Subject Areas

ATP-dependent proteolysis, Non-native membrane proteins, Periplasmic domain, Crystal structure, Photosystem II.

Readers' Comments and Ratings (0)

Leave a public comment
Send a private comment to the author(s)
Rate this article
Views 0
Downloads 0
Comments 0
Metrics 0
Leave a public comment

×
Alerts
Notify me about updates to this article or when a peer-reviewed version is published.