3G71

Co-crystal structure of Bruceantin bound to the large ribosomal subunit

Summary for 3G71

• Entry DOI: 10.2210/pdb3g71/pdb
• Related: 3G4S 3G6E
• Descriptor: 23S ribosomal RNA, 50S ribosomal protein L11P, 50S ribosomal protein L13P, ... (39 entities in total)
• Functional Keywords: large ribosomal subunit, haloarcula marismortui, bruceantin, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, metal-binding, zinc-finger, ribosome
• Biological source: Haloarcula marismortui; More
• Cellular location: Cytoplasm : P12743
• Total number of polymer chains: 31
• Total formula weight: 1461630.46

Authors

Gurel, G.,Blaha, G.,Moore, P.B.,Steitz, T.A. (deposition date: 2009-02-09, release date: 2009-04-28, Last modification date: 2023-09-06)

Primary citation

Gurel, G.,Blaha, G.,Moore, P.B.,Steitz, T.A.
U2504 determines the species specificity of the A-site cleft antibiotics: the structures of tiamulin, homoharringtonine, and bruceantin bound to the ribosome.
J.Mol.Biol., 389:146-156, 2009

PubMed Abstract: Structures have been obtained for the complexes that tiamulin, homoharringtonine, and bruceantin form with the large ribosomal subunit of Haloarcula marismortui at resolutions ranging from 2.65 to 3.2 A. They show that all these inhibitors block protein synthesis by competing with the amino acid side chains of incoming aminoacyl-tRNAs for binding in the A-site cleft in the peptidyl-transferase center, which is universally conserved. In addition, these structures support the hypothesis that the species specificity exhibited by the A-site cleft inhibitors is determined by the interactions they make, or fail to make, with a single nucleotide, U2504 (Escherichia coli). In the ribosome, the position of U2504 is controlled by its interactions with neighboring nucleotides, whose identities vary among kingdoms.

PubMed: 19362093
DOI: 10.1016/j.jmb.2009.04.005

Experimental method

X-RAY DIFFRACTION (2.85 Å)