6sj5
Crystal structure of the uL14-RsfS complex from Staphylococcus aureusCrystal structure of the uL14-RsfS complex from Staphylococcus aureus
Structural highlights
FunctionW8TVV3_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 PubMedFor 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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