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1ffk, resolution 2.40Å ()
Ligands: , ,
Related: 1c04
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Publication Abstract from PubMed

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.

The complete atomic structure of the large ribosomal subunit at 2.4 A resolution., Ban N, Nissen P, Hansen J, Moore PB, Steitz TA, Science. 2000 Aug 11;289(5481):905-20. PMID:10937989

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1ffk is a 28 chain structure with sequence from Haloarcula marismortui. The October 2000 RCSB PDB Molecule of the Month feature on Ribosome by David S. Goodsell is 10.2210/rcsb_pdb/mom_2000_10. Full crystallographic information is available from OCA.

See Also


  • Ban N, Nissen P, Hansen J, Moore PB, Steitz TA. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science. 2000 Aug 11;289(5481):905-20. PMID:10937989
  • Nissen P, Ippolito JA, Ban N, Moore PB, Steitz TA. RNA tertiary interactions in the large ribosomal subunit: the A-minor motif. Proc Natl Acad Sci U S A. 2001 Apr 24;98(9):4899-903. Epub 2001 Apr 10. PMID:11296253 doi:10.1073/pnas.081082398
  • Rawat UB, Zavialov AV, Sengupta J, Valle M, Grassucci RA, Linde J, Vestergaard B, Ehrenberg M, Frank J. A cryo-electron microscopic study of ribosome-bound termination factor RF2. Nature. 2003 Jan 2;421(6918):87-90. PMID:12511960 doi:10.1038/nature01224
  • Valle M, Zavialov A, Li W, Stagg SM, Sengupta J, Nielsen RC, Nissen P, Harvey SC, Ehrenberg M, Frank J. Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy. Nat Struct Biol. 2003 Nov;10(11):899-906. Epub 2003 Oct 19. PMID:14566331 doi:10.1038/nsb1003

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