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TitleInterplay between an ATP-binding cassette F protein and the ribosome from Mycobacterium tuberculosis.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 432, Year 2022
Publish dateJan 21, 2022
AuthorsZhicheng Cui / Xiaojun Li / Joonyoung Shin / Howard Gamper / Ya-Ming Hou / James C Sacchettini / Junjie Zhang /
PubMed AbstractEttA, 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 linksNat Commun / PubMed:35064151 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.71 - 3.23 Å
Structure data

EMDB-23961, PDB-7msc:
Mtb 70SIC in complex with MtbEttA at Pre_R0 state
Method: EM (single particle) / Resolution: 2.97 Å

EMDB-23962, PDB-7msh:
Mtb 70SIC in complex with MtbEttA at Pre_R1 state
Method: EM (single particle) / Resolution: 3.23 Å

EMDB-23969, PDB-7msm:
Mtb 70SIC in complex with MtbEttA at Trans_R0 state
Method: EM (single particle) / Resolution: 2.79 Å

EMDB-23972, PDB-7msz:
Mtb 70SIC in complex with MtbEttA at Trans_R1 state
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-23974, PDB-7mt2:
Mtb 70S initiation complex
Method: EM (single particle) / Resolution: 2.76 Å

EMDB-23975, PDB-7mt3:
Mtb 70S with P/E tRNA
Method: EM (single particle) / Resolution: 2.8 Å

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 analogue*YM

ChemComp-FME:
N-FORMYLMETHIONINE

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-VO4:
VANADATE ION

Source
  • mycobacterium tuberculosis h37rv (bacteria)
  • mycobacterium tuberculosis (strain atcc 25618 / h37rv) (bacteria)
  • escherichia coli (E. coli)
  • mycobacterium tuberculosis (bacteria)
KeywordsRIBOSOME / mycobacterium tuberculosis / ABCF ribosome complex / antibiotic / HYDROLASE

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