5hl7

The crystal structure of the large ribosomal subunit of Staphylococcus aureus in complex with lefamulin

spinqualitylabelsall models 5hl7, resolution 3.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5hl7 is a 10 chain structure with sequence from Staphylococcus aureus subsp. aureus NCTC 8325. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.55Å Ligands: 62B, EOH, EPE, MG, MN, MPD, SPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL3_STAA8 One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. Publication Abstract from PubMed The increasing appearance of pathogenic bacteria with antibiotic resistance is a global threat. Consequently, clinically available potent antibiotics that are active against multidrug resistant pathogens are becoming exceedingly scarce. Ribosomes are a main target for antibiotics, and hence are an objective for novel drug development. Lefamulin, a semi-synthetic pleuromutilin compound highly active against multi-resistant pathogens, is a promising antibiotic currently in phase III trials for the treatment of community-acquired bacterial pneumonia in adults. The crystal structure of the Staphylococcus aureus large ribosomal subunit in complex with lefamulin reveals its protein synthesis inhibition mechanism and the rationale for its potency. In addition, analysis of the bacterial and eukaryotes ribosome structures around the pleuromutilin binding pocket has elucidated the key for the drug's selectivity. A novel pleuromutilin antibacterial compound, its binding mode and selectivity mechanism.,Eyal Z, Matzov D, Krupkin M, Paukner S, Riedl R, Rozenberg H, Zimmerman E, Bashan A, Yonath A Sci Rep. 2016 Dec 13;6:39004. doi: 10.1038/srep39004. PMID:27958389 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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