Structural studies on Helicobacter pyloriATP-dependent protease, FtsH.

Journal of Synchrotron Radiation
Sung Hyun KimS H Eom

Abstract

The ATP-dependent protease, FtsH, degrades misassembled membrane proteins for quality control like SecY, subunit a of FoF1-ATPase, and YccA, and digests short-lived soluble proteins in order to control their cellular regulation, including sigma32, LpxC and lambdacII. The FtsH protein has an N-terminal transmembrane segment and a large cytosolic region that consists of two domains, an ATPase and a protease domain. To provide a structural basis for the nucleotide-dependent domain motions and a better understanding of substrate translocation, the crystal structures of the Helicobacter pylori (Hp) FtsH ATPase domain in the nucleotide-free state and complexed with ADP, were determined. Two different structures of HpFtsH ATPase were observed, with the nucleotide-free state in an asymmetric unit, and these structures reveal the new forms and show other conformational differences between the nucleotide-free and ADP-bound state compared with previous structures. In particular, one HpFtsH Apo structure has a considerable rotation difference compared with the HpFtsH ADP complex, and this large conformational change reveals that FtsH may have the mechanical force needed for substrate translocation.

References

Jan 1, 1996·Annual Review of Genetics·S Gottesman
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May 25, 2005·Annual Review of Microbiology·Koreaki Ito, Yoshinori Akiyama
Feb 18, 2006·Proceedings of the National Academy of Sciences of the United States of America·Christoph BieniossekUlrich Baumann
Jun 10, 2006·Molecular Cell·Ryoji SunoKosuke Morikawa

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Citations

Sep 20, 2011·Biochimica Et Biophysica Acta·Sina LangklotzFranz Narberhaus
Nov 7, 2020·The Journal of Biological Chemistry·Vanessa CarvalhoMarie-Eve Aubin-Tam
Jan 19, 2021·The Journal of Biological Chemistry·Vanessa CarvalhoMarie-Eve Aubin-Tam

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