1ffk
From Proteopedia
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'''CRYSTAL STRUCTURE OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI AT 2.4 ANGSTROM RESOLUTION''' | '''CRYSTAL STRUCTURE OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI AT 2.4 ANGSTROM RESOLUTION''' | ||
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[[Category: Nissen, P.]] | [[Category: Nissen, P.]] | ||
[[Category: Steitz, T A.]] | [[Category: Steitz, T A.]] | ||
| - | [[Category: | + | [[Category: Protein-protein]] |
| - | [[Category: | + | [[Category: Protein-rna]] |
| - | [[Category: | + | [[Category: Ribosome assembly]] |
| - | [[Category: | + | [[Category: Rna-rna]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:15:55 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:15, 2 May 2008
CRYSTAL STRUCTURE OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI AT 2.4 ANGSTROM RESOLUTION
Overview
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.
About this Structure
1FFK is a Protein complex structure of sequences from Haloarcula marismortui. The following page contains interesting information on the relation of 1FFK with [Ribosome]. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 16:15:55 2008
