Structures of triacetyloleandomycin and mycalamide A bind to the large ribosomal subunit of Haloarcula marismortui

Antimicrob Agents Chemother. 2009 Dec;53(12):5010-4. doi: 10.1128/AAC.00817-09. Epub 2009 Sep 8.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Crystallography, X-Ray
  • Haloarcula marismortui / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding / drug effects
  • Protein Biosynthesis / drug effects
  • Pyrans / chemistry*
  • Pyrans / pharmacology*
  • Ribosome Subunits, Large / chemistry*
  • Ribosome Subunits, Large / metabolism*
  • Troleandomycin / chemistry*
  • Troleandomycin / pharmacology*

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Pyrans
  • mycalamide A
  • Troleandomycin

Associated data

  • PDB/3I55-6