4u25

Crystal structure of the E. coli ribosome bound to virginiamycin M1.

spinqualitylabelsall models 4u25, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4u25 is a 20 chain structure with sequence from Escherichia coli K-12. This structure supersedes the now removed PDB entries 4tp4, 4tp5, 4tp6 and 4tp7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: MG, VIR, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RS16_ECOLI In addition to being a ribosomal protein, S16 also has a cation-dependent endonuclease activity. In-frame fusions with the ribosome maturation factor rimM suppress mutations in the latter (probably due to increased rimM expression) and are found in translationally active 70S ribosomes. Publication Abstract from PubMed Streptogramin antibiotics are divided into type A and B streptogramins, which in combination can act synergistically. We compared the molecular interactions of the streptogramin combinations Synercid (type A: dalfopristin, type B: quinupristin) and NXL 103 (type A: flopristin, type B: linopristin) with the Escherichia coli 70S ribosome by x-ray crystallography. We further analyzed the activity of the streptogramin components individually and in combination. Streptogramin A and B components in Synercid and NXL 103 exhibit synergistic antimicrobial activity against certain pathogenic bacteria. However, in transcription-coupled translation assays, only combinations that include dalfopristin, the streptogramin A component of Synercid, show synergy. Notably, the diethylaminoethylsulfonyl group in dalfopristin reduces its activity, but is the basis for synergy in transcription-coupled translation assays before its rapid hydrolysis from the depsipeptide core. Replacement of the diethylaminoethylsulfonyl group in dalfopristin by a non-hydrolyzable group may therefore be beneficial for synergy. The absence of general streptogramin synergy in transcription-coupled translation assays suggests that synergistic antimicrobial activity of streptogramins can occur independently of streptogramin effects on translation. Synergy of streptogramin antibiotics occurs independently of their effects on translation.,Noeske J, Huang J, Olivier NB, Giacobbe RA, Zambrowski M, Cate JH Antimicrob Agents Chemother. 2014 Jun 23. pii: AAC.03389-14. PMID:24957822 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosome 3D structures

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