EMD-30611
Cryo-EM map of 70S ribosome in complex with peptide deformylase, trigger factor, and methionine aminopeptidase
EMD-30611
Single-particle4.1 Å
Deposition: 06/10/2020Map released: 07/04/2021
Last modified: 29/05/2024
Sample Organism:
Escherichia coli,
Escherichia coli (strain K12)
Sample: E. coli 70S ribosome in complex with enzyme peptide deformylase, chaperone trigger factor, and enzyme methionine aminopeptidase
Fitted models: 7d80 (Avg. Q-score: 0.339)
Deposition Authors: Akbar S, Bhakta S
Sample: E. coli 70S ribosome in complex with enzyme peptide deformylase, chaperone trigger factor, and enzyme methionine aminopeptidase
Fitted models: 7d80 (Avg. Q-score: 0.339)
Deposition Authors: Akbar S, Bhakta S
Structural insights into the interplay of protein biogenesis factors with the 70S ribosome.
Abstract:
Bacterial co-translational N-terminal methionine excision, an early event of nascent polypeptide chain processing, is mediated by two enzymes: peptide deformylase (PDF) and methionine aminopeptidase (MetAP). Trigger factor (TF), the only ribosome-associated bacterial chaperone, offers co-translational chaperoning assistance. Here, we present two high-resolution cryoelectron microscopy structures of tRNA-bound E. coli ribosome complexes showing simultaneous binding of PDF and TF, in the absence (3.4 Å) and presence of MetAP (4.1 Å). These structures establish molecular details of the interactions of the factors with the ribosome, and thereby reveal the structural basis of nascent chain processing. Our results suggest that simultaneous binding of all three factors is not a functionally favorable mechanism of nascent chain processing. Strikingly, an unusual structural distortion of the 70S ribosome, potentially driven by binding of multiple copies of MetAP, is observed when MetAP is incubated with a pre-formed PDF-TF-bound ribosome complex.
Bacterial co-translational N-terminal methionine excision, an early event of nascent polypeptide chain processing, is mediated by two enzymes: peptide deformylase (PDF) and methionine aminopeptidase (MetAP). Trigger factor (TF), the only ribosome-associated bacterial chaperone, offers co-translational chaperoning assistance. Here, we present two high-resolution cryoelectron microscopy structures of tRNA-bound E. coli ribosome complexes showing simultaneous binding of PDF and TF, in the absence (3.4 Å) and presence of MetAP (4.1 Å). These structures establish molecular details of the interactions of the factors with the ribosome, and thereby reveal the structural basis of nascent chain processing. Our results suggest that simultaneous binding of all three factors is not a functionally favorable mechanism of nascent chain processing. Strikingly, an unusual structural distortion of the 70S ribosome, potentially driven by binding of multiple copies of MetAP, is observed when MetAP is incubated with a pre-formed PDF-TF-bound ribosome complex.