Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Interplay between an ATP-binding cassette F protein and the ribosome from Mycobacterium tuberculosis.
Journal, issue, pages	Nat Commun, Vol. 13, Issue 1, Page 432, Year 2022
Publish date	Jan 21, 2022
Authors	Zhicheng Cui / Xiaojun Li / Joonyoung Shin / Howard Gamper / Ya-Ming Hou / James C Sacchettini / Junjie Zhang /
PubMed Abstract	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 ...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-VO) 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-VO 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.
External links	Nat Commun / PubMed:35064151 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2.71 - 3.23 Å
Structure data	23961 7msc EMDB-23961, PDB-7msc: Mtb 70SIC in complex with MtbEttA at Pre_R0 state Method: EM (single particle) / Resolution: 2.97 Å 23962 7msh EMDB-23962, PDB-7msh: Mtb 70SIC in complex with MtbEttA at Pre_R1 state Method: EM (single particle) / Resolution: 3.23 Å 23969 7msm EMDB-23969, PDB-7msm: Mtb 70SIC in complex with MtbEttA at Trans_R0 state Method: EM (single particle) / Resolution: 2.79 Å 23972 7msz EMDB-23972, PDB-7msz: Mtb 70SIC in complex with MtbEttA at Trans_R1 state Method: EM (single particle) / Resolution: 3.1 Å 23974 7mt2 EMDB-23974, PDB-7mt2: Mtb 70S initiation complex Method: EM (single particle) / Resolution: 2.76 Å 23975 7mt3 EMDB-23975, PDB-7mt3: Mtb 70S with P/E tRNA Method: EM (single particle) / Resolution: 2.8 Å 23976 7mt7 EMDB-23976, PDB-7mt7: Mtb 70S with P and E site tRNAs Method: EM (single particle) / Resolution: 2.71 Å EMDB-23981: Mtb 50S Method: EM (single particle) / Resolution: 3.0 Å PDB-7mu0: MtbEttA in the ADP bound state Method: X-RAY DIFFRACTION / Resolution: 2.9 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-MG: Unknown entry ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogueYM ChemComp-FME: N-FORMYLMETHIONINE ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-VO4: VANADATE ION
Source	mycobacterium tuberculosis h37rv (bacteria) mycobacterium tuberculosis (strain atcc 25618 / h37rv) (bacteria) escherichia coli (E. coli) mycobacterium tuberculosis (bacteria)
Keywords	RIBOSOME / mycobacterium tuberculosis / ABCF ribosome complex / antibiotic / HYDROLASE