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Structural Analysis of 70S Ribosomes by Cross-Linking/Mass Spectrometry Reveals Conformational Plasticity

ABSTRACT: We analyzed 143 E. coli ribosomal structures, mapping a total of 10,771 intramolecular distances for 126 cross-link-pairs and 3,405 intermolecular distances for 97 protein pairs. Our study might serve as benchmark for conducting biochemical experiments on newly modeled protein regions, guided by XL-MS.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Escherichia Coli

SUBMITTER: Daniele Ubbiali

LAB HEAD: Andrea Sinz

PROVIDER: PXD018935 | Pride | 2020-08-13

REPOSITORIES: Pride

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Structural analysis of 70S ribosomes by cross-linking/mass spectrometry reveals conformational plasticity.

Tüting Christian C Iacobucci Claudio C Ihling Christian H CH Kastritis Panagiotis L PL Sinz Andrea A

Scientific reports 20200728 1

The ribosome is not only a highly complex molecular machine that translates the genetic information into proteins, but also an exceptional specimen for testing and optimizing cross-linking/mass spectrometry (XL-MS) workflows. Due to its high abundance, ribosomal proteins are frequently identified in proteome-wide XL-MS studies of cells or cell extracts. Here, we performed in-depth cross-linking of the E. coli ribosome using the amine-reactive cross-linker disuccinimidyl diacetic urea (DSAU). We ...[more]

PMID: 32724211

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