Structures of triacetyloleandomycin and mycalamide A bind to the large ribosomal subunit of Haloarcula marismortui.
Structures have been obtained for the complexes that triacetyloleandomycin and mycalamide A form with the large ribosomal subunit of Haloarcula marismortui. Triacetyloleandomycin binds in the nascent peptide tunnel and inhibits the activity of ribosomes by blocking the growth of the nascent peptide chain. Mycalamide A binds to the E site and inhibits protein synthesis by occupying the space normally occupied by the CCA end of E-site-bound tRNAs.
Gürel
Güliz
G
Department of Chemistry, Yale University, New Haven, CT 06520, USA.
Blaha
Gregor
G
Steitz
Thomas A
TA
Moore
Peter B
PB
D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000494:pharmacology; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D019614:Haloarcula marismortui / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding / Q000187:drug effects; D014176:Protein Biosynthesis / Q000187:drug effects; D011714:Pyrans / Q000737:chemistry* / Q000494:pharmacology*; D054658:Ribosome Subunits, Large / Q000737:chemistry* / Q000378:metabolism*; D014217:Troleandomycin / Q000737:chemistry* / Q000494:pharmacology*
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D011714:Pyrans; C059646:mycalamide A; D014217:Troleandomycin