3CC2

The Refined Crystal Structure of the Haloarcula Marismortui Large Ribosomal Subunit at 2.4 Angstrom Resolution with rrnA Sequence for the 23S rRNA and Genome-derived Sequences for r-Proteins

Summary for 3CC2

• Entry DOI: 10.2210/pdb3cc2/pdb
• Related: 1FFK 1S72 3CC4 3CC7 3CCE 3CCJ 3CCL 3CCM 3CCQ 3CCR 3CCS 3CCU 3CCV 3CD6
• Descriptor: 50S ribosomal protein L2P, 50S ribosomal protein L13P, 50S ribosomal protein L14P, ... (37 entities in total)
• Functional Keywords: genomic sequnece for r-proteins, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, metal-binding, zinc-finger, ribosome
• Biological source: Haloarcula marismortui (Halobacterium marismortui); More
• Total number of polymer chains: 31
• Total formula weight: 1484613.81

Authors

Gurel, G.,Blaha, G. (deposition date: 2008-02-23, release date: 2008-05-20, Last modification date: 2024-02-21)

Primary citation

Blaha, G.,Gurel, G.,Schroeder, S.J.,Moore, P.B.,Steitz, T.A.
Mutations outside the anisomycin-binding site can make ribosomes drug-resistant.
J.Mol.Biol., 379:505-519, 2008

PubMed Abstract: Eleven mutations that make Haloarcula marismortui resistant to anisomycin, an antibiotic that competes with the amino acid side chains of aminoacyl tRNAs for binding to the A-site cleft of the large ribosomal unit, have been identified in 23S rRNA. The correlation observed between the sensitivity of H. marismortui to anisomycin and the affinity of its large ribosomal subunits for the drug indicates that its response to anisomycin is determined primarily by the binding of the drug to its large ribosomal subunit. The structures of large ribosomal subunits containing resistance mutations show that these mutations can be divided into two classes: (1) those that interfere with specific drug-ribosome interactions and (2) those that stabilize the apo conformation of the A-site cleft of the ribosome relative to its drug-bound conformation. The conformational effects of some mutations of the second kind propagate through the ribosome for considerable distances and are reversed when A-site substrates bind to the ribosome.

PubMed: 18455733
DOI: 10.1016/j.jmb.2008.03.075

Experimental method

X-RAY DIFFRACTION (2.4 Å)