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The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution
Nenad Ban,1*Poul Nissen,1*Jeffrey Hansen,1Peter B. Moore,12Thomas A. Steitz123
The large ribosomal subunit catalyzes peptide bond formation and
binds initiation, termination, and elongation factors. Wehave
determined the crystal structure of the large ribosomal subunitfrom
Haloarcula marismortui at 2.4 angstrom resolution, and itincludes 2833 of the subunit's 3045 nucleotides and 27 of its31 proteins. The domains of its RNAs all have irregular shapesand fit
together in the ribosome like the pieces of a three-dimensionaljigsaw
puzzle to form a large, monolithic structure. Proteinsare abundant
everywhere on its surface except in the active sitewhere peptide bond
formation occurs and where it contacts thesmall subunit. Most of the
proteins stabilize the structure byinteracting with several RNA
domains, often using idiosyncraticallyfolded extensions that reach
into the subunit's interior.
1 Department of Molecular Biophysics & Biochemistry, and
2 Department of Chemistry, Yale
University, and
3 Howard Hughes Medical Institute,
New Haven, CT 06520-8114, USA.
*
These two authors contributed equally to this work.
The editors suggest the following Related Resources on Science sites:
In Science Magazine
PERSPECTIVES
Thomas R. Cech (11 August 2000) Science289 (5481), 878.
[DOI: 10.1126/science.289.5481.878] |Summary »|Full Text »
RESEARCH ARTICLES
Poul Nissen, Jeffrey Hansen, Nenad Ban, Peter B. Moore, and Thomas A. Steitz (11 August 2000) Science289 (5481), 920.
[DOI: 10.1126/science.289.5481.920] |Abstract »|Full Text »|PDF »
REPORTS
Gregory W. Muth, Lori Ortoleva-Donnelly, and Scott A. Strobel (11 August 2000) Science289 (5481), 947.
[DOI: 10.1126/science.289.5481.947] |Abstract »|Full Text »|PDF »
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