Publication Date:
2009-10-20
Description:
The high-resolution structures of ribosomal subunits published in 2000 have revolutionized the field of protein translation. They facilitated the determination and interpretation of functional complexes of the ribosome by crystallography and electron microscopy. Knowledge of the precise positions of residues in the ribosome in various states has facilitated increasingly sophisticated biochemical and genetic experiments, as well as the use of new methods such as single-molecule kinetics. In this review, we discuss how the interaction between structural and functional studies over the last decade has led to a deeper understanding of the complex mechanisms underlying translation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmeing, T Martin -- Ramakrishnan, V -- MC_U105184332/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- Wellcome Trust/United Kingdom -- England -- Nature. 2009 Oct 29;461(7268):1234-42. doi: 10.1038/nature08403. Epub 2009 Oct 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK. schmeing@mrc-lmb.cam.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19838167" target="_blank"〉PubMed〈/a〉
Keywords:
Bacterial Proteins/chemistry/metabolism
;
Biocatalysis
;
Protein Biosynthesis/*physiology
;
Ribosomal Proteins/metabolism
;
Ribosomes/*chemistry/*metabolism
;
Structure-Activity Relationship
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
