7mu0

MtbEttA in the ADP bound state

spinqualitylabelsall models 7mu0, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7mu0 is a 2 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: ADP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ETTA_MYCTU 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. ATP hydrolysis probably frees it from the ribosome, which can enter the elongation phase.[HAMAP-Rule:MF_00847] Publication Abstract from PubMed EttA, energy-dependent translational throttle A, is a ribosomal factor that gates ribosome entry into the translation elongation cycle. A detailed understanding of its mechanism of action is limited due to the lack of high-resolution structures along its ATPase cycle. Here we present the cryo-electron microscopy (cryo-EM) structures of EttA from Mycobacterium tuberculosis (Mtb), referred to as MtbEttA, in complex with the Mtb 70S ribosome initiation complex (70SIC) at the pre-hydrolysis (ADPNP) and transition (ADP-VO4) states, and the crystal structure of MtbEttA alone in the post-hydrolysis (ADP) state. We observe that MtbEttA binds the E-site of the Mtb 70SIC, remodeling the P-site tRNA and the ribosomal intersubunit bridge B7a during the ribosomal ratcheting. In return, the rotation of the 30S causes conformational changes in MtbEttA, forcing the two nucleotide-binding sites (NBSs) to alternate to engage each ADPNP in the pre-hydrolysis states, followed by complete engagements of both ADP-VO4 molecules in the ATP-hydrolysis transition states. In the post-hydrolysis state, the conserved ATP-hydrolysis motifs of MtbEttA dissociate from both ADP molecules, leaving two nucleotide-binding domains (NBDs) in an open conformation. These structures reveal a dynamic interplay between MtbEttA and the Mtb ribosome, providing insights into the mechanism of translational regulation by EttA-like proteins. Interplay between an ATP-binding cassette F protein and the ribosome from Mycobacterium tuberculosis.,Cui Z, Li X, Shin J, Gamper H, Hou YM, Sacchettini JC, Zhang J Nat Commun. 2022 Jan 21;13(1):432. doi: 10.1038/s41467-022-28078-1. PMID:35064151 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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