PDBsum entry 4ww0

Hydrolase

PDB id: 4ww0

Contents

Protein chains

420 a.a.

Ligands

ADP ×3

Metals

_ZN ×3

Waters ×3

PDB id:

4ww0

Name:

Hydrolase

Title:

Truncated ftsh from a. Aeolicus

Structure:

Atp-dependent zinc metalloprotease ftsh. Chain: a, b, c. Fragment: unp residues 142-634. Engineered: yes. Mutation: yes

Source:

Aquifex aeolicus. Organism_taxid: 224324. Strain: vf5. Gene: ftsh, aq_936. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: rosetta.

Resolution:

2.96Å R-factor: 0.211 R-free: 0.248

Authors:

M.Vostrukhina,U.Baumann,M.Schacherl,C.Bieniossek,M.Lanz,R.Baumgartner

Key ref:

M.Vostrukhina et al. (2015). The structure of Aquifex aeolicus FtsH in the ADP-bound state reveals a C2-symmetric hexamer. Acta Crystallogr D Biol Crystallogr, 71, 1307-1318. PubMed id: 26057670 DOI: 10.1107/S1399004715005945

Date:

09-Nov-14 Release date: 06-May-15

Protein chains

O67077  (FTSH_AQUAE) -  ATP-dependent zinc metalloprotease FtsH from Aquifex aeolicus (strain VF5)

Seq: 634 a.a.

Struc: 420 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.4.24.- - ?????

DOI no: 10.1107/S1399004715005945

Acta Crystallogr D Biol Crystallogr 71:1307-1318 (2015)

PubMed id: 26057670

The structure of Aquifex aeolicus FtsH in the ADP-bound state reveals a C2-symmetric hexamer.

M.Vostrukhina, A.Popov, E.Brunstein, M.A.Lanz, R.Baumgartner, C.Bieniossek, M.Schacherl, U.Baumann.

ABSTRACT

The crystal structure of a truncated, soluble quadruple mutant of FtsH from Aquifex aeolicus comprising the AAA and protease domains has been determined at 2.96 Å resolution in space group I222. The protein crystallizes as a hexamer, with the protease domain forming layers in the ab plane. Contacts between these layers are mediated by the AAA domains. These are highly disordered in one crystal form, but are clearly visible in a related form with a shorter c axis. Here, adenosine diphosphate (ADP) is bound to each subunit and the AAA ring exhibits twofold symmetry. The arrangement is different from the ADP-bound state of an analogously truncated, soluble FtsH construct from Thermotoga maritima. The pore is completely closed and the phenylalanine residues in the pore line a contiguous path. The protease hexamer is very similar to those described for other FtsH structures. To resolve certain open issues regarding a conserved glycine in the linker between the AAA and protease domains, as well as the active-site switch β-strand, mutations have been introduced in the full-length membrane-bound protein. Activity analysis of these point mutants reveals the crucial importance of these residues for proteolytic activity and is in accord with previous interpretation of the active-site switch and the importance of the linker glycine residue.