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Atomic structures at last: the ribosome in 2000.

V Ramakrishnan¹, P B Moore

¹Medical Research Council Laboratory of Molecular Biology, Cambridge, UK. ramak@mrc-lmb.cam.ac.uk

Current Opinion in Structural Biology

|April 12, 2001

Summary

Recent atomic structures of ribosomal subunits from Haloarcula marismortui and Thermus thermophilus are revolutionizing protein synthesis understanding. These findings provide unprecedented insights into the ribosome

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Area of Science:

Structural biology
Molecular biology
Biochemistry

Background:

The ribosome is a crucial molecular machine responsible for protein synthesis.
Previous studies provided lower-resolution structural information of ribosomal subunits.

Purpose of the Study:

To present high-resolution atomic structures of the 50S and 30S ribosomal subunits.
To advance the understanding of the ribosome's structure and function in protein synthesis.

Main Methods:

X-ray crystallography was used to determine the atomic structures.
Cryo-electron microscopy provided a lower-resolution map of the 70S ribosome.

Main Results:

Atomic structures of the 50S ribosomal subunit from Haloarcula marismortui were determined.

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Atomic structures of the 30S ribosomal subunit from Thermus thermophilus were determined.

A 7.8 A resolution electron density map of the 70S ribosome from T. thermophilus was obtained.

Conclusions:

These high-resolution structures are revolutionizing our understanding of protein synthesis.
The detailed structural information facilitates mechanistic studies of translation.