4fin

From Proteopedia

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

Structural highlights

4fin is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ETTA_ECOLI A translation factor that gates the progression of the 70S ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site) into the translation elongation cycle by using a mechanism sensitive to the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates the state of the translating ribosome during subunit translocation. Stimulates dipeptide bond synthesis in the presence of ATP (cell in high energy state), but inhibits dipeptide synthesis in the presence of ADP (cell in low energy state), and thus may control translation in response to changing ATP levels (including during stationary phase). Following ATP hydrolysis is probably released allowing the ribosome to enter the elongation phase. ATPase activity is stimulated in the presence of ribosomes. Its specificity for the IC may be conferred by its recognition of features unique to tRNA(fMet).^[1] ^[2]

Publication Abstract from PubMed

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.

The ABC-F protein EttA gates ribosome entry into the translation elongation cycle.,Boel G, Smith PC, Ning W, Englander MT, Chen B, Hashem Y, Testa AJ, Fischer JJ, Wieden HJ, Frank J, Gonzalez RL Jr, Hunt JF Nat Struct Mol Biol. 2014 Jan 5. doi: 10.1038/nsmb.2740. PMID:24389466^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chen B, Boel G, Hashem Y, Ning W, Fei J, Wang C, Gonzalez RL Jr, Hunt JF, Frank J. EttA regulates translation by binding the ribosomal E site and restricting ribosome-tRNA dynamics. Nat Struct Mol Biol. 2014 Jan 5. doi: 10.1038/nsmb.2741. PMID:24389465 doi:http://dx.doi.org/10.1038/nsmb.2741
↑ Boel G, Smith PC, Ning W, Englander MT, Chen B, Hashem Y, Testa AJ, Fischer JJ, Wieden HJ, Frank J, Gonzalez RL Jr, Hunt JF. The ABC-F protein EttA gates ribosome entry into the translation elongation cycle. Nat Struct Mol Biol. 2014 Jan 5. doi: 10.1038/nsmb.2740. PMID:24389466 doi:http://dx.doi.org/10.1038/nsmb.2740
↑ Boel G, Smith PC, Ning W, Englander MT, Chen B, Hashem Y, Testa AJ, Fischer JJ, Wieden HJ, Frank J, Gonzalez RL Jr, Hunt JF. The ABC-F protein EttA gates ribosome entry into the translation elongation cycle. Nat Struct Mol Biol. 2014 Jan 5. doi: 10.1038/nsmb.2740. PMID:24389466 doi:http://dx.doi.org/10.1038/nsmb.2740