4wcw

Ribosomal silencing factor during starvation or stationary phase (RsfS) from Mycobacterium tuberculosis

spinqualitylabelsall models 4wcw, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wcw is a 4 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: MG, MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O86327_MYCTU 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 (By similarity).[HAMAP-Rule:MF_01477] Publication Abstract from PubMed The ribosomal silencing factor RsfS slows cell growth by inhibiting protein synthesis during periods of diminished nutrient availability. The crystal structure of Mycobacterium tuberculosis (Mtb) RsfS, together with the cryo-electron microscopy (EM) structure of the large subunit 50S of Mtb ribosome, reveals how inhibition of protein synthesis by RsfS occurs. RsfS binds to the 50S at L14, which, when occupied, blocks the association of the small subunit 30S. Although Mtb RsfS is a dimer in solution, only a single subunit binds to 50S. The overlap between the dimer interface and the L14 binding interface confirms that the RsfS dimer must first dissociate to a monomer in order to bind to L14. RsfS interacts primarily through electrostatic and hydrogen bonding to L14. The EM structure shows extended rRNA density that it is not found in the Escherichia coli ribosome, the most striking of these being the extended RNA helix of H54a. Structure of Ribosomal Silencing Factor Bound to Mycobacterium tuberculosis Ribosome.,Li X, Sun Q, Jiang C, Yang K, Hung LW, Zhang J, Sacchettini JC Structure. 2015 Aug 19. pii: S0969-2126(15)00320-2. doi:, 10.1016/j.str.2015.07.014. PMID:26299947 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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