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Science 11 August 2000:
Vol. 289. no. 5481, pp. 905 - 920
DOI: 10.1126/science.289.5481.905
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Research Articles

The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution

Nenad Ban,1* Poul Nissen,1* Jeffrey Hansen,1 Peter B. Moore,12 Thomas A. Steitz123dagger

The large ribosomal subunit catalyzes peptide bond formation and binds initiation, termination, and elongation factors. We have determined the crystal structure of the large ribosomal subunit from Haloarcula marismortui at 2.4 angstrom resolution, and it includes 2833 of the subunit's 3045 nucleotides and 27 of its 31 proteins. The domains of its RNAs all have irregular shapes and fit together in the ribosome like the pieces of a three-dimensional jigsaw puzzle to form a large, monolithic structure. Proteins are abundant everywhere on its surface except in the active site where peptide bond formation occurs and where it contacts the small subunit. Most of the proteins stabilize the structure by interacting with several RNA domains, often using idiosyncratically folded 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.

dagger    To whom correspondence should be addressed.

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Science. ISSN 0036-8075 (print), 1095-9203 (online)