6sj5

Crystal structure of the uL14-RsfS complex from Staphylococcus aureus

spinqualitylabelsall models 6sj5, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6sj5 is a 4 chain structure with sequence from Staphylococcus aureus and 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 2.2668655Å Ligands: ACY, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W8TVV3_STAAU Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.[HAMAP-Rule:MF_01477] Publication Abstract from PubMed For the sake of energy preservation, bacteria, upon transition to stationary phase, tone down their protein synthesis. This process is favored by the reversible binding of small stress-induced proteins to the ribosome to prevent unnecessary translation. One example is the conserved bacterial ribosome silencing factor (RsfS) that binds to uL14 protein onto the large ribosomal subunit and prevents its association with the small subunit. Here we describe the binding mode of Staphylococcus aureus RsfS to the large ribosomal subunit and present a 3.2 A resolution cryo-EM reconstruction of the 50S-RsfS complex together with the crystal structure of uL14-RsfS complex solved at 2.3 A resolution. The understanding of the detailed landscape of RsfS-uL14 interactions within the ribosome shed light on the mechanism of ribosome shutdown in the human pathogen S. aureus and might deliver a novel target for pharmacological drug development and treatment of bacterial infections. Mechanism of ribosome shutdown by RsfS in Staphylococcus aureus revealed by integrative structural biology approach.,Khusainov I, Fatkhullin B, Pellegrino S, Bikmullin A, Liu WT, Gabdulkhakov A, Shebel AA, Golubev A, Zeyer D, Trachtmann N, Sprenger GA, Validov S, Usachev K, Yusupova G, Yusupov M Nat Commun. 2020 Apr 3;11(1):1656. doi: 10.1038/s41467-020-15517-0. PMID:32245971 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein L14

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