2R62: Crystal Structure Of Helicobacter Pylori Atp Dependent Protease, Ftsh

Citation:
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.
PDB ID: 2R62Download
MMDB ID: 66552
PDB Deposition Date: 2007/9/5
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 3.3  Å
Source Organism:
Similar Structures:
Biological Unit for 2R62: monomeric; determined by author and by software (PISA)
Molecular Components in 2R62
Label Count Molecule
Protein (1 molecule)
1
Cell Division Protease Ftsh Homolog(Gene symbol: HP1069)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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