The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation

B11 BAUMANN/ZAUCKEpublicationsBieniossek, C., Niederhauser, B., and Baumann, U., Proc Natl Acad Sci U S A. 2009 Dec 22;106(51):21579-84. doi: 10.1073/pnas.0910708106. Epub 2009 Dec 2.


The hexameric membrane-spanning ATP-dependent metalloprotease FtsH is universally conserved in eubacteria, mitochondria, and chloroplasts, where it fulfills key functions in quality control and signaling. As a member of the self-compartmentalizing ATPases associated with various cellular activities (AAA+ proteases), FtsH converts the chemical energy stored in ATP via conformational rearrangements into a mechanical force that is used for substrate unfolding and translocation into the proteolytic chamber. The crystal structure of the ADP state of Thermotoga maritima FtsH showed a hexameric assembly consisting of a 6-fold symmetric protease disk and a 2-fold symmetric AAA ring. The 2.6 A resolution structure of the cytosolic region of apo-FtsH presented here reveals a new arrangement where the ATPase ring shows perfect 6-fold symmetry with the crucial pore residues lining an open circular entrance. Triggered by this conformational change, a substrate-binding edge beta strand appears within the proteolytic domain. Comparison of the apo- and ADP-bound structure visualizes an inward movement of the aromatic pore residues and generates a model of substrate translocation by AAA+ proteases. Furthermore, we demonstrate that mutation of a conserved glycine in the linker region inactivates FtsH.



  • Upcoming Events

    1. Cologne Seminars on Ageing Series 2018 with Elaine Fuchs

      März 6 @ 4:00 pm - 5:30 pm
    2. SFB 829 Connector Meeting

      April 6 @ 3:00 pm - 5:30 pm
    3. SFB 829 Connector Meeting

      August 31 @ 3:00 pm - 5:30 pm
    4. International Symposium „Molecular Mechanisms regulating Skin Homeostasis“

      November 12 - November 14
    5. SFB 829 Connector Meeting

      Dezember 7 @ 3:00 pm - 5:30 pm
  • News

© 2017 SFB 829