4FIN

Crystal Structure of EttA (formerly YjjK) - an E. coli ABC-type ATPase

Summary for 4FIN

• Entry DOI: 10.2210/pdb4fin/pdb
• Descriptor: EttA (YjjK) ABCF family protein, SULFATE ION, CITRIC ACID, ... (6 entities in total)
• Functional Keywords: abc protein, abcf, mechanoenzyme, gating of ribosomal elongation, ribosome, cytosol/ribosome, atp-binding protein, northeast structural genomics consortium, nesg, psi-biology, structural genomics
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 128223.29

Authors

Smith, P.,Yuan, Y.,Hunt, J.F.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2012-06-09, release date: 2013-07-03, Last modification date: 2024-11-20)

Primary citation

Boel, G.,Smith, P.C.,Ning, W.,Englander, M.T.,Chen, B.,Hashem, Y.,Testa, A.J.,Fischer, J.J.,Wieden, H.J.,Frank, J.,Gonzalez, R.L.,Hunt, J.F.
The ABC-F protein EttA gates ribosome entry into the translation elongation cycle.
Nat.Struct.Mol.Biol., 21:143-151, 2014

PubMed 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.

PubMed: 24389466
DOI: 10.1038/nsmb.2740

Experimental method

X-RAY DIFFRACTION (2.4 Å)