PDBsum entry 1iy0

Hydrolase

PDB id: 1iy0

Contents

Protein chain

240 a.a. *

Ligands

ANP

* Residue conservation analysis

PDB id:

1iy0

Name:

Hydrolase

Title:

Crystal structure of the ftsh atpase domain with amp-pnp from thermus thermophilus

Structure:

Atp-dependent metalloprotease ftsh. Chain: a. Fragment: f1. Engineered: yes

Source:

Thermus thermophilus. Organism_taxid: 274. Gene: ftsh. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.95Å R-factor: 0.225 R-free: 0.289

Authors:

H.Niwa,D.Tsuchiya,H.Makyio,M.Yoshida,K.Morikawa

Key ref:

H.Niwa et al. (2002). Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8. Structure, 10, 1415-1423. PubMed id: 12377127 DOI: 10.1016/S0969-2126(02)00855-9

Date:

10-Jul-02 Release date: 06-Nov-02

Protein chain

Q5SI82  (FTSH_THET8) -  ATP-dependent zinc metalloprotease FtsH from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

Seq: 624 a.a.

Struc: 240 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.4.24.- - ?????

DOI no: 10.1016/S0969-2126(02)00855-9

Structure 10:1415-1423 (2002)

PubMed id: 12377127

Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8.

H.Niwa, D.Tsuchiya, H.Makyio, M.Yoshida, K.Morikawa.

ABSTRACT

FtsH is a cytoplasmic membrane-integrated, ATP-dependent metalloprotease, which processively degrades both cytoplasmic and membrane proteins in concert with unfolding. The FtsH protein is divided into the N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. We have determined the crystal structures of the Thermus thermophilus FtsH ATPase domain in the nucleotide-free and AMP-PNP- and ADP-bound states, in addition to the domain with the extra preceding segment. Combined with the mapping of the putative substrate binding region, these structures suggest that FtsH internally forms a hexameric ring structure, in which ATP binding could cause a conformational change to facilitate transport of substrates into the protease domain through the central pore.

Selected figure(s)

Figure 3.
Figure 3. Hexameric Ring Model of the FtsH ATPase Domain(A) The figures are viewed from the transmembrane side (left) and the protease domain side (right). From the extra segment position of the FtsH-F2 crystal structure, we found that the transmembrane helices are located on the N-terminal side of the hexagonal plate. The model possesses an outer diameter of approximately 120 Å, with a central pore of 13 Å in diameter. Note the gap between subunits, which becomes narrow in comparison with that in the crystal packing arrangement, as shown in Figure 1D. The rotation angle between subdomains in the model differs by 34° from that in the crystal. Although every subunit is represented with the same conformation in this model, the mode of the ATPase cycle, either sequential or synchronized, cannot be clarified.(B) Representation of the arginine finger in the model viewed from the transmembrane side. Arg313 is located at a position capable of interacting with the g-phosphate of AMP-PNP bound to a neighboring subunit. The SRH motif, highlighted in pink, is located on the contact surface between subunits. The a7 helix and the following loop in front of Arg313 are eliminated.(C) SRH motif in the model, viewed from the protease domain side. The motif from the AMP-PNP form is superimposed onto that from the ADP form. The Ca atom of Asn302 is colored red.(D) Mapping of the putative substrate binding regions (brown). Note that the MFVG sequence (green) faces the central pore. A closed line indicates a monomer structure, corresponding to the highlighted one in (A).(E) Electrostatic potential surfaces of the model, calculated by the program GRASP [52]. Red and blue represent regions of negative and positive potential, respectively.

The above figure is reprinted by permission from Cell Press: Structure (2002, 10, 1415-1423) copyright 2002.

Figure was selected by an automated process.