PDBsum entry: 2dhr

Hydrolase

PDB id: 2dhr

Contents

Protein chains

(+ 0 more) 458 a.a. *

Ligands

ADP ×6

* Residue conservation analysis

PDB id:

2dhr

Name:

Hydrolase

Title:

Whole cytosolic region of atp-dependent metalloprotease ftsh (g399l)

Structure:

Ftsh. Chain: a, b, c, d, e, f. Fragment: whole cytosolic region. Synonym: atp-dependent metalloprotease. Engineered: yes. Mutation: yes

Source:

Thermus thermophilus. Organism_taxid: 274. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Hexamer (from PQS)

Resolution:

3.90Å R-factor: 0.301 R-free: 0.342

Authors:

R.Suno,H.Niwa,D.Tsuchiya,X.Zhang,M.Yoshida,K.Morikawa

Key ref:

R.Suno et al. (2006). Structure of the whole cytosolic region of ATP-dependent protease FtsH. Mol Cell, 22, 575-585. PubMed id: 16762831 DOI: 10.1016/j.molcel.2006.04.020

Date:

24-Mar-06 Release date: 27-Jun-06

Protein chain

Q9LCZ4  (Q9LCZ4_THETH) -

 Gene Ontology (GO) functional annotation 

• Cellular component: membrane (1 term)
• Biological process: protein catabolic process (2 terms)
• Biochemical function: nucleotide binding (4 terms)

DOI no: 10.1016/j.molcel.2006.04.020

Mol Cell 22:575-585 (2006)

PubMed id: 16762831

Structure of the whole cytosolic region of ATP-dependent protease FtsH.

R.Suno, H.Niwa, D.Tsuchiya, X.Zhang, M.Yoshida, K.Morikawa.

ABSTRACT

An ATP-dependent protease, FtsH, digests misassembled membrane proteins in order to maintain membrane integrity and digests short-lived soluble proteins in order to control their cellular regulation. This enzyme has an N-terminal transmembrane segment and a C-terminal cytosolic region consisting of an AAA+ ATPase domain and a protease domain. Here we present two crystal structures: the protease domain and the whole cytosolic region. The cytosolic region fully retains an ATP-dependent protease activity and adopts a three-fold-symmetric hexameric structure. The protease domains displayed a six-fold symmetry, while the AAA+ domains, each containing ADP, alternate two orientations relative to the protease domain, making "open" and "closed" interdomain contacts. Apparently, ATPase is active only in the closed form, and protease operates in the open form. The protease catalytic sites are accessible only through a tunnel following from the AAA+ domain of the adjacent subunit, raising a possibility of translocation of polypeptide substrate to the protease sites through this tunnel.

Selected figure(s)

Figure 4.
Figure 4. Catalytic Environments in sFtsH

Figure 6.
Figure 6. The ATPase Cycle and Putative Polypeptide Translocation Pathway

The above figures are reprinted by permission from Cell Press: Mol Cell (2006, 22, 575-585) copyright 2006.

Figures were selected by the author.