1NKW

Crystal Structure Of The Large Ribosomal Subunit From Deinococcus Radiodurans

Replaces:  1LNRReplaces:  1KC9Replaces:  1KPJ

Summary for 1NKW

• Entry DOI: 10.2210/pdb1nkw/pdb
• Related: 1JZX 1JZY 1JZZ 1K00 1K01 1NJM 1NJN 1NJO 1NJP
• Descriptor: 23S ribosomal RNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (31 entities in total)
• Functional Keywords: ribosome; large subunit; 50s; deinococcus radiodurans; x-ray structure; peptidyl-transferase, peptide bond formation, ribosome
• Biological source: Deinococcus radiodurans; More
• Total number of polymer chains: 31
• Total formula weight: 1388100.24

Authors

Harms, J.M.,Schluenzen, F.,Zarivach, R.,Bashan, A.,Gat, S.,Agmon, I.,Bartels, H.,Franceschi, F.,Yonath, A. (deposition date: 2003-01-05, release date: 2003-02-11, Last modification date: 2023-08-16)

Primary citation

Harms, J.M.,Schluenzen, F.,Zarivach, R.,Bashan, A.,Gat, S.,Agmon, I.,Bartels, H.,Franceschi, F.,Yonath, A.
High resolution structure of the large ribosomal subunit from a mesophilic eubacterium
Cell(Cambridge,Mass.), 107:679-688, 2001

PubMed Abstract: We describe the high resolution structure of the large ribosomal subunit from Deinococcus radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and functionally relevant ligands. The over-all structure of D50S is similar to that from the archae bacterium Haloarcula marismortui (H50S); however, a detailed comparison revealed significant differences, for example, in the orientation of nucleotides in peptidyl transferase center and in the structures of many ribosomal proteins. Analysis of ribosomal features involved in dynamic aspects of protein biosynthesis that are partially or fully disordered in H50S revealed the conformations of intersubunit bridges in unbound subunits, suggesting how they may change upon subunit association and how movements of the L1-stalk may facilitate the exit of tRNA.

PubMed: 11733066
DOI: 10.1016/S0092-8674(01)00546-3

Experimental method

X-RAY DIFFRACTION (3.1 Å)