PDBsum entry 4fin

Atp-binding protein

PDB id: 4fin

Contents

Protein chains

538 a.a.

Ligands

SO4 ×11

CIT

PGE

GOL ×9

Waters ×396

PDB id:

4fin

Name:

Atp-binding protein

Title:

Crystal structure of etta (formerly yjjk) - an e. Coli abc-type atpase

Structure:

Etta (yjjk) abcf family protein. Chain: a, b. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k-12. Gene: b4391, jw4354, yjjk, yjjk. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.40Å R-factor: 0.186 R-free: 0.243

Authors:

P.Smith,Y.Yuan,J.F.Hunt,Northeast Structural Genomics Consortium (Nesg)

Key ref:

G.Boël et al. (2014). The ABC-F protein EttA gates ribosome entry into the translation elongation cycle. Nat Struct Biol, 21, 143-151. PubMed id: 24389466 DOI: 10.1038/nsmb.2740

Date:

09-Jun-12 Release date: 03-Jul-13

Protein chains

P0A9W3  (ETTA_ECOLI) -  Energy-dependent translational throttle protein EttA from Escherichia coli (strain K12)

Seq: 555 a.a.

Struc: 538 a.a.

Enzyme reactions

• Enzyme class: E.C.3.6.1.- - ?????

DOI no: 10.1038/nsmb.2740

Nat Struct Biol 21:143-151 (2014)

PubMed id: 24389466

The ABC-F protein EttA gates ribosome entry into the translation elongation cycle.

G.Boël, P.C.Smith, W.Ning, M.T.Englander, B.Chen, Y.Hashem, A.J.Testa, J.J.Fischer, H.J.Wieden, J.Frank, R.L.Gonzalez, J.F.Hunt.

ABSTRACT

ABC-F proteins have evaded functional characterization even though they compose one of the most widely distributed branches of the ATP-binding cassette (ABC) superfamily. Herein, we demonstrate that YjjK, the most prevalent eubacterial ABC-F protein, gates ribosome entry into the translation elongation cycle through a nucleotide-dependent interaction sensitive to ATP/ADP ratio. Accordingly, we rename this protein energy-dependent translational throttle A (EttA). We determined the crystal structure of Escherichia coli EttA and used it to design mutants for biochemical studies including enzymological assays of the initial steps of protein synthesis. These studies suggest that EttA may regulate protein synthesis in energy-depleted cells, which have a low ATP/ADP ratio. Consistently with this inference, EttA-deleted cells exhibit a severe fitness defect in long-term stationary phase. These studies demonstrate that an ABC-F protein regulates protein synthesis via a new mechanism sensitive to cellular energy status.