PDBsum entry 3kds

Metal binding protein

PDB id: 3kds

Contents

Protein chains

427 a.a. *

Ligands

NHX ×3

Metals

_ZN ×3

* Residue conservation analysis

PDB id:

3kds

Name:

Metal binding protein

Title:

Apo-ftsh crystal structure

Structure:

Cell division protein ftsh. Chain: e, f, g. Fragment: cytosolic region, residues 146-610. Engineered: yes. Mutation: yes

Source:

Thermotoga maritima. Organism_taxid: 2336. Gene: ftsh. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.60Å R-factor: 0.226 R-free: 0.287

Authors:

C.Bieniossek,B.Niederhauser,U.Baumann

Key ref:

C.Bieniossek et al. (2009). The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation. Proc Natl Acad Sci U S A, 106, 21579-21584. PubMed id: 19955424

Date:

23-Oct-09 Release date: 01-Dec-09

Protein chains

Q9WZ49  (FTSH_THEMA) -  ATP-dependent zinc metalloprotease FtsH from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

Seq: 610 a.a.

Struc: 427 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.4.24.- - ?????

Proc Natl Acad Sci U S A 106:21579-21584 (2009)

PubMed id: 19955424

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

C.Bieniossek, B.Niederhauser, U.M.Baumann.

ABSTRACT

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.