New study reveals more details of ribosome

from the Pocket-Change dept.

Researchers have obtained the most detailed images yet of catalytic site of the ribosome, the factory where amino acids are linked into chainlike proteins.

In two articles published in the 11 August 2000 issue of Science, researchers led by Thomas A. Steitz, a Howard Hughes Medical Institute investigator at Yale University, report that they have obtained the atomic structure of the 50S subunit of the ribosome at a resolution of 2.4 Ångströms.

A press release describes the studies of the basic structure of the ribosome, which includes the first unequivocal proof that the ribosome is a ribozyme, an RNA enzyme.

According to Steitz, the latest high-resolution structure offers a pathway to far deeper understanding of the protein-assembling machinery. The researchers are planning further studies to understand how the messenger RNA and components of the growing protein are oriented in the ribosome's catalytic active site. They will also explore how the ribosome structure influences the chemical properties of the molecular groups in the active site. And, the scientists will seek to understand how the multitude of magnesium and potassium ions and water molecules integrate into the ribosome and stabilize it.

More information about the research team can be found through this Yale University press release. And there is also a popular article available online from Science News.

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